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
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1.8.4.10
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aeruginosa
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sulfur
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thioredoxins
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reductases
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gamma-glutamylcysteine
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physcomitrella
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moss
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thiosulfate
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assimilatory
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patens
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two-electron
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analysis
- 1.8.4.10
- aeruginosa
- sulfur
- thioredoxins
- reductases
- gamma-glutamylcysteine
-
physcomitrella
-
moss
- thiosulfate
-
assimilatory
- patens
-
two-electron
- analysis
Reaction
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
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Crystallization
Crystallization on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)
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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
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crystal structure is consistent with a preference for adenosine 5'-phosphosulfate. The [Fe4-S4] cluster enhances the enzyme's activity