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2JI1

X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009636biological_processresponse to toxic substance
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046872molecular_functionmetal ion binding
A0050605molecular_functionsuperoxide reductase activity
B0005506molecular_functioniron ion binding
B0009636biological_processresponse to toxic substance
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
B0050605molecular_functionsuperoxide reductase activity
C0005506molecular_functioniron ion binding
C0009636biological_processresponse to toxic substance
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0046872molecular_functionmetal ion binding
C0050605molecular_functionsuperoxide reductase activity
D0005506molecular_functioniron ion binding
D0009636biological_processresponse to toxic substance
D0016491molecular_functionoxidoreductase activity
D0019430biological_processremoval of superoxide radicals
D0046872molecular_functionmetal ion binding
D0050605molecular_functionsuperoxide reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A1127
ChainResidue
ACYS10
ACYS13
ACYS29
ACYS30

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A1128
ChainResidue
AGLU18
AHOH2042
AHOH2043
BHOH2193
BHOH2196

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1129
ChainResidue
AASP33
AHOH2074
AHOH2076
CGLU26
CHOH2051
CHOH2064

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A1130
ChainResidue
AHIS49
AHIS69
AHIS75
ACYS116
AHIS119

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B1127
ChainResidue
BCYS10
BCYS13
BCYS29
BCYS30

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B1128
ChainResidue
BHIS49
BHIS69
BHIS75
BCYS116
BHIS119

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE C1127
ChainResidue
CCYS10
CCYS13
CCYS29
CCYS30

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C1128
ChainResidue
AASP33
AHOH2057
CGLU26
CASP33
CHOH2068
CHOH2069

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C1129
ChainResidue
CGLU18
CHOH2039
CHOH2136
DHOH2142

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 C1130
ChainResidue
CHIS49
CHIS69
CHIS75
CCYS116
CHIS119

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE D1127
ChainResidue
DCYS10
DCYS13
DCYS29
DCYS30

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 D1128
ChainResidue
DHIS49
DHIS69
DHIS75
DCYS116
DHIS119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1do6
ChainResidueDetails
ALYS48
AGLU47

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1do6
ChainResidueDetails
BLYS48
BGLU47

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1do6
ChainResidueDetails
CLYS48
CGLU47

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1do6
ChainResidueDetails
DLYS48
DGLU47

246704

PDB entries from 2025-12-24

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