1.8.1.8: protein-disulfide reductase
This is an abbreviated version!
For detailed information about protein-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.8
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1.8.1.8
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thioredoxins
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gsh
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monothiol
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ribonucleotide
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peroxiredoxins
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deglutathionylation
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glutathione-dependent
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redox-active
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reductases
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thiol-disulfide
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iron-sulfur
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fe-s
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redox-sensitive
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thioltransferase
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trx1
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thioredoxin-like
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dehydroascorbate
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nadph-dependent
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cys
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hydroperoxide
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deoxyribonucleotides
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selenoenzyme
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auranofin
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bola
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thioredoxin-dependent
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redox-dependent
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selenocysteine
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gsh-dependent
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trypanothione
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thiol-based
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diamide
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oxidoreduction
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dtnb
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peroxidases
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redox-regulated
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sulfenic
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dsba
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ask1
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poplar
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selenoproteins
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sideroblast
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thiol-dependent
- 1.8.1.8
- thioredoxins
- gsh
- monothiol
- ribonucleotide
- peroxiredoxins
-
deglutathionylation
-
glutathione-dependent
-
redox-active
- reductases
-
thiol-disulfide
-
iron-sulfur
- fe-s
-
redox-sensitive
- thioltransferase
- trx1
-
thioredoxin-like
- dehydroascorbate
-
nadph-dependent
- cys
- hydroperoxide
- deoxyribonucleotides
-
selenoenzyme
- auranofin
-
bola
-
thioredoxin-dependent
-
redox-dependent
- selenocysteine
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gsh-dependent
- trypanothione
-
thiol-based
- diamide
-
oxidoreduction
- dtnb
- peroxidases
-
redox-regulated
-
sulfenic
- dsba
- ask1
- poplar
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selenoproteins
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sideroblast
-
thiol-dependent
Reaction
Synonyms
AhpF, disulfide reductase, EC 1.6.4.4, ERdj5, ERp16, glutaredoxin, HvTrxh2, insulin-glutathione transhydrogenase, LpdA, MA3736, MA_1658, MdrA, methanoredoxin, More, NAD(P)H:protein-disulfide oxidoreductase, NADH-linked disulfide reductase, panthethine 4'4-diphosphate-specific reductase, PDI reductase, PDO, PfPDO, PH1130 protein, PhDsb, protein disulfide isomerase reductase, protein disulfide oxidoreductase, protein disulfide reductase, protein-disulfide oxidoreductase, protein-disulfide reductase (NAD(P)H), reductase, protein disulfide, thiol-disulfide oxidoreductase, TON_0319, TTC0486, WhiB1, WhiB1/Rv3219
ECTree
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Crystallization
Crystallization on EC 1.8.1.8 - protein-disulfide reductase
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crystal structure exhibits a classic thioredoxin-glutaredoxin fold comprising three alpha-helices surrounding four antiparallel beta-sheets. The crystal lattice has four monomers in a dimer of dimers arrangement. A cadmium ion is found within the active site of each monomer, and two cadmium ions stabilize the N-terminal tails and dimer interfaces. CoMSH and glutathione bind to the active site of methanoredoxin similar to the binding of glutathione in glutaredoxin
sitting drop vapor diffusion method, using 10% (w/v) PEG 8000, 100 mM HEPES (pH 7.5), and 8 mM cystin at 20°C
purified recombinant His-tagged enzyme LpdA, hanging drop vapour diffusion method at room temperature, 0.003 ml protein solution containing 25 mg/ml protein, 10 mM HEPES, pH 7.5, mixed with 0.002 ml precipitant solution containing 0.1 M trisodium citrate, pH 5.4-5.8, 2.5-5.0% PEG 6000, 3-7 days depending on the pH, crystallization takes longer at higher pH-value, crystals are immersed in 10% PEG 6000, 100 mM MES, pH 5.75, and 25% glycerol, X-ray diffraction structure determination and analysis at 2.8 A resolution
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sitting-drop vapor diffusion method, crystals belong to the hexagonal space group P6522 with cell dimensions of a = b = 110.3 and c = 68.5 and with one molecule in the asymmtric unit. The structure is solved by multiple isomorphous replacement including anomalous scattering data. The structure is refined to 1.9 resolution
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analysis of the X-ray structure at 2.0 A resolution
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