1.8.1.B5: protein-disulfide reductase (CoM-dependent)

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For detailed information about protein-disulfide reductase (CoM-dependent), go to the full flat file.

Reaction

Synonyms

MA_1658, methanoredoxin

ECTree

     1 Oxidoreductases

         1.8 Acting on a sulfur group of donors

             1.8.1 With NAD⁺ or NADP⁺ as acceptor

                1.8.1.B5 protein-disulfide reductase (CoM-dependent)

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Results	in table
1	AA Sequence
2	Cofactor
1	Crystallization (Commentary)
2	KM Value [mM]
1	Metals/Ions
2	Molecular Weight [Da]
3	Organism
1	Reaction
2	Reference
6	Substrates and Products (Substrate)
2	Subunits
4	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 1.8.1.B5 - protein-disulfide reductase (CoM-dependent)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure exhibits a classic thioredoxin-glutaredoxin fold comprising three alpha-helices surrounding four antiparallel beta-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to glutaredoxins. Active site modeling of coenzyme M shows the sulfate moiety hydrogen-bonded to the backbone amide and carbonyl oxygen of residue Phe 76

Methanosarcina acetivorans

Q8TQ93

733364