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2O8V

PAPS reductase in a covalent complex with thioredoxin C35A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004604molecular_functionphosphoadenylyl-sulfate reductase (thioredoxin) activity
A0005737cellular_componentcytoplasm
A0006790biological_processsulfur compound metabolic process
A0016491molecular_functionoxidoreductase activity
A0019379biological_processsulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
A0070814biological_processhydrogen sulfide biosynthetic process
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0015035molecular_functionprotein-disulfide reductase activity
B0015036molecular_functiondisulfide oxidoreductase activity
B0030337molecular_functionDNA polymerase processivity factor activity
B0045454biological_processcell redox homeostasis
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
BCYS32
BALA35

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
BASP26

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
BGLY33
BPRO34

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
BLYS69

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cqg
ChainResidueDetails
BALA35
BCYS32

site_idMCSA1
Number of Residues3
DetailsM-CSA 279
ChainResidueDetails
AASP206electrostatic stabiliser, hydrogen bond donor
ALEU210electrostatic stabiliser, hydrogen bond donor
AGLY240activator, covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor

222926

PDB entries from 2024-07-24

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