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Information on EC 1.5.1.42 - FMN reductase (NADH)
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1.5.1.42 FMN reductase (NADH)IUBMB Comments
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
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Word Map
- 1.5.1.42
- luciferase
- monooxygenase
-
desulfurization
-
bioluminescent
- rhodococcus
-
biodesulfurization
- erythropolis
-
photobacterium
- dibenzothiophene
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fossil
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instantly
- p-hydroxyphenylacetate
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cost-competitive
- baumannii
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sigma54-dependent
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petroleum
-
fmnh2-dependent
- phosphoreum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
nadh-fmn oxidoreductase, hcba3, nadh:fmn-oxidoreductase, nadh-dependent fmn reductase, nadh specific fmn reductase, nadh-fmn reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DszD
flavin reductase
Fred
hexachlorobenzene oxidative dehalogenase system reductase component
UniProt
LuxG
LuxG oxidoreductase
NADH specific FMN reductase
NADH-dependent FMN reductase
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-
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NADH-FMN oxidoreductase
NADH-FMN reductase
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NADH:flavin oxidoreductase
NADH:FMN oxidoreductase
NADH:flavin oxidoreductase
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NADH:FMN oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NAD+ = FMN + NADH + H+
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-
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FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
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FMNH2 + NAD+ = FMN + NADH + H+
catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview
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FMNH2 + NAD+ = FMN + NADH + H+
HcbA3 follows a ping-pong bi-bi mechanism for the reduction of flavins
FMNH2 + NAD+ = FMN + NADH + H+
catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview
Rhodococcus erythropolis IGTS8 / ATCC 53968
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-
FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
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SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD+ oxidoreductase
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FAD + NADH + H+
FADH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
-
-
?
FAD + NADH + H+
FADH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FAD + NADH + H+
FADH2 + NAD+
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activity with FADH2 and NAD+ is 5% of the activity with FMNH2 and NAD+
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FMN + NADH + H+
FMNH2 + NAD+
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activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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?
FMN + NADH + H+
FMNH2 + NAD+
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the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
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?
FMN + NADH + H+
FMNH2 + NAD+
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the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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?
FMN + NADPH + H+
FMNH2 + NADP+
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activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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?
FMN + NADPH + H+
FMNH2 + NADP+
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the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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?
additional information
?
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HcbA3 is an NADH:FMN oxidoreductase. Successful reconstitution of the oxidative dehalogenase reaction in vitro, which consists of HcbA1, HcbA3, FMN, and NADH, suggesting that HcbA3 may also be the partner reductase component for HcbA1 in Nocardioides sp. PD653. The optimal molar ratio of HcbA1 and HcbA3 is 7:1
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additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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?
additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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?
additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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?
additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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?
additional information
?
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establishment of a coupled pure enzyme bioluminescent system and usage for quantitative detection, method evaluation
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-
additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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-
?
additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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-
?
additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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-
?
additional information
?
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establishment of a coupled pure enzyme bioluminescent system and usage for quantitative detection, method evaluation
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-
-
additional information
?
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activity with FAD and NADPH is 0.5% of the activity with FMNH2 and NAD+
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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-
?
additional information
?
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-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
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-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADH
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the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
NADPH
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activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADPH
-
the NADH specific FMN reductase does does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no inhibition by: 0.000325 M dicoumarol, 10 mM KCN, 1% Triton X-100
-
additional information
-
no inhibition by 0.01 mM 2,4-dinitrophenol, 0.2 mM dicoumarol, 0.1 mM rotenone
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Riboflavin Deficiency
Effect of riboflavin deficiency on activity of NADH-FMN oxidoreductase (ferriductase) and iron content of rat liver.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
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additional information
additional information
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the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
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additional information
additional information
Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme
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additional information
additional information
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Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme
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additional information
additional information
steady-state kinetic analysis, the initial rates of NADH oxidation follow typical Michaelis-Menten kinetics, and Lineweaver-Burk plots show parallel patterns for a ping-pong mechanism
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s
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additional information
additional information
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LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
purity was too low to permit estimation of specific activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
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bimodal, pH 5: 90% of maximal activity, pH 6.5: about 50% of maximal activity, pH 10: about 70% of maximal activity
5 - 8.6
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the pH curve is bimodal, with maximal activity exhibited at pH 8.6, a minimum at pH 6.0. and a second maximum at pH 5.0
7 - 8.6
at pH 7.0, 7.2, and 8.0, the enzyme activity levels in 100 mM phosphate buffer are approx. 50.2, 88.1, and 81.1%, respectively, relative to that at pH 7.5. HcbA3C-His shows the highest flavin reductase activity in 60 mM KPi buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
additional information
additional information
stopped-flow kinetic experiments are performed at 4°C
additional information
-
stopped-flow kinetic experiments are performed at 4°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
mutation of the critical residue Thr62, T62N and T62A, show a 5 and 7fold increase in catalytic rate, respectively
metabolism
physiological function
additional information
evolution
phylogenetic analysis demonstrats that Photobacterium leiognathi strain YL LuxG has a rather distant evolutionary relationship with Frase I of Aliivibrio fischeri and Frp of Vibrio harveyi, but a close evolutionary relationship with Fre from Escherichia coli, which are all enzymes related to oxidoreductases. Changes in the functionally conserved sites contribute to the functional divergence of LuxG and Fre. Bioinformatics analysis of LuxG sequences in bacteria, overview. Structure comparisons
evolution
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phylogenetic analysis demonstrats that Photobacterium leiognathi strain YL LuxG has a rather distant evolutionary relationship with Frase I of Aliivibrio fischeri and Frp of Vibrio harveyi, but a close evolutionary relationship with Fre from Escherichia coli, which are all enzymes related to oxidoreductases. Changes in the functionally conserved sites contribute to the functional divergence of LuxG and Fre. Bioinformatics analysis of LuxG sequences in bacteria, overview. Structure comparisons
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metabolism
the enzyme is involved in the degradation of (-)-camphor
metabolism
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the enzyme is involved in the degradation of (-)-camphor
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physiological function
bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview
physiological function
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NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence
physiological function
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Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC
physiological function
DszD from Rhodococcus erythropolis is a NADH-FMN oxidoreductase responsible for supplying FMNH2 to DszA and DszC in the biodesulfurization process of crude oil, the 4S pathway. The rate-limiting step of the reduction of FMN to FMNH2 is a process catalysed by DszD and known to play an important role in the reaction energy profile
physiological function
LuxG supplies reduced flavin mononucleotide (FMN) for bacterial luminescence by catalyzing the oxidation of nicotinamide adenine dinucleotide hydrogen (NADH)
physiological function
Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). HcbA3 shows the highest affinity for FMN. HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653
physiological function
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC
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physiological function
-
bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview
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physiological function
-
LuxG supplies reduced flavin mononucleotide (FMN) for bacterial luminescence by catalyzing the oxidation of nicotinamide adenine dinucleotide hydrogen (NADH)
-
additional information
-
the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A
additional information
critical role of the residue in position 62 (threonine) of the DszD sequence in the enzymatic activity. This residue is located near the N5 atom of the isoalloxazine ring of FMN. Structure modelling of wild-type and mutants using quantum mechanics/molecular mechanics (QM/MM) method, and active site as well as substrate binding structure analysis, overview
additional information
-
critical role of the residue in position 62 (threonine) of the DszD sequence in the enzymatic activity. This residue is located near the N5 atom of the isoalloxazine ring of FMN. Structure modelling of wild-type and mutants using quantum mechanics/molecular mechanics (QM/MM) method, and active site as well as substrate binding structure analysis, overview
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A
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