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4L05

Cu/Zn superoxide dismutase from Brucella abortus

Replaces:  2AQM
Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0005615cellular_componentextracellular space
A0006801biological_processsuperoxide metabolic process
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU1 A 201
ChainResidue
AHIS48
AHIS50
AHIS73
AHIS128
AHOH562

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 202
ChainResidue
AHOH562
AHIS48
AHIS50
AHIS73
AHIS128

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 203
ChainResidue
AHIS73
AHIS82
AHIS90
AASP93

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
APRO76
AARG123
AHOH348
AHOH447
AHOH474
AHOH529

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
ATHR3
ATHR4
AHOH426

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEnPScA
ChainResidueDetails
AGLY46-ALA56

site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GGGGaRfACgvI
ChainResidueDetails
AGLY142-ILE153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS48
AHIS50
AHIS73
AHIS82
AHIS90
AASP93
AHIS128

219140

PDB entries from 2024-05-01

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