1.8.4.10: adenylyl-sulfate reductase (thioredoxin)

This is an abbreviated version!
For detailed information about adenylyl-sulfate reductase (thioredoxin), go to the full flat file.

Word Map on EC 1.8.4.10

Reaction

AMP
+
sulfite
+
thioredoxin disulfide
=
5'-adenylyl sulfate
+
thioredoxin

Synonyms

5'-adenylylsulfate reductase, adenosine-5'-phosphosulfate reductase, adenylylsulfate reductase, APR, APR-B, APS reductase, PaAPR, PpAPR-B, thioredoxin dependent 5'-adenylylsulfate reductase, thioredoxin-dependent APS reductase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.10 adenylyl-sulfate reductase (thioredoxin)

Crystallization

Crystallization on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)

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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
virtual ligand docking simulations with inhibitors. For 2-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-[(2-sulfanylethyl)amino]-9H-purin-9-yl]oxolan-2-yl]ethyl phosphate, the AMP scaffold binds within the substrate-binding pocket and establishes interactions with key active site residues
-
crystal structure is consistent with a preference for adenosine 5'-phosphosulfate. The [Fe4-S4] cluster enhances the enzyme's activity