Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:9405149
ChainResidueDetails
AHIS44
AHIS46
AHIS61
AHIS69
AHIS78
AASP81
AHIS118

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon