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1S3C

ARSENATE REDUCTASE C12S MUTANT FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0008794molecular_functionarsenate reductase (glutaredoxin) activity
A0016491molecular_functionoxidoreductase activity
A0046685biological_processresponse to arsenic-containing substance
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
ASER12
AHOH1131
AGLY13
ATHR14
AARG60
AASN62
AARG94
AARG107
AHOH1008
AHOH1063

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AARG60
AARG60
AASN62
AASN62
AHOH1101

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
ATHR14
AASN17
APRO108
ASER109
ALYS126
AHOH1035
AHOH1070
AHOH1106
AHOH1111

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CS A 301
ChainResidue
ALEU113
ALEU113
AASP114
AASP114
ALEU116
ALEU116

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS A 302
ChainResidue
APRO38
AGLU43
AHOH1157

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS A 303
ChainResidue
AGLU64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; cysteine thioarsenate intermediate => ECO:0000255|PROSITE-ProRule:PRU01282, ECO:0000269|PubMed:11709171, ECO:0000269|PubMed:15295115, ECO:0000269|PubMed:7577935
ChainResidueDetails
ASER12

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Important for activity. Lowers pKa of the active site Cys => ECO:0000269|PubMed:8969183
ChainResidueDetails
AHIS8

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Important for activity. Involved in arsenate binding and transition-state stabilization => ECO:0000269|PubMed:11709171, ECO:0000269|PubMed:14592722, ECO:0000269|PubMed:15295115
ChainResidueDetails
AARG60
AARG94
AARG107

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PDB entries from 2024-06-12

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