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1IB5

X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT W83Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AHIS70
AHIS79
AHIS88
AASP91

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 202
ChainResidue
AHIS45
AHIS47
AHIS70
AHIS125
AHOH214

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHQnGScA
ChainResidueDetails
AGLY43-ALA53

site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GGGGaRvACgvI
ChainResidueDetails
AGLY139-ILE150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AHIS45
AHIS47
AHIS70
AHIS79
AHIS88
AASP91
AHIS125

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AARG144
AHIS70

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS70

227561

PDB entries from 2024-11-20

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