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1ESO

MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0006801biological_processsuperoxide metabolic process
A0008270molecular_functionzinc ion binding
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 149
ChainResidue
AHIS69
AHIS78
AASP81
AHIS61

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 150
ChainResidue
AHIS44
AHIS46
AHIS61
AHIS118

site_idCUL
Number of Residues4
DetailsCU LIGANDS.
ChainResidue
AHIS44
AHIS46
AHIS61
AHIS118

site_idZNL
Number of Residues4
DetailsZN LIGANDS.
ChainResidue
AHIS61
AHIS69
AHIS78
AASP81

Functional Information from PROSITE/UniProt
site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GGGGeRyACgvI
ChainResidueDetails
AGLY136-ILE147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9405149","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 6316150, 10026301
ChainResidueDetails
AHIS61

246704

PDB entries from 2025-12-24

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