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2ET1

Oxalate oxidase in complex with substrate analogue glycolate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0030145molecular_functionmanganese ion binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0048046cellular_componentapoplast
A0050162molecular_functionoxalate oxidase activity
A0071555biological_processcell wall organization
A1902693cellular_componentsuperoxide dismutase complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 202
ChainResidue
AHIS88
AHIS90
AGLU95
AHIS137
AGLV203
AHOH221

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GLV A 203
ChainResidue
AHIS88
AHIS90
AGLU95
AMET149
AMN202
AHOH221
AHOH333
AASN75
AVAL77
AASN85

Functional Information from PROSITE/UniProt
site_idPS00725
Number of Residues14
DetailsGERMIN Germin family signature. GtnppHiHPrAtEI
ChainResidueDetails
AGLY83-ILE96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ETE
ChainResidueDetails
AASN75

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16291738, ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ETE
ChainResidueDetails
AASN85
AHIS90

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11062559, ECO:0000269|PubMed:16291738, ECO:0007744|PDB:1FI2, ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ET7, ECO:0007744|PDB:2ETE
ChainResidueDetails
AHIS88
AHIS137

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16291738, ECO:0007744|PDB:2ETE
ChainResidueDetails
AGLU95

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16291738, ECO:0007744|PDB:2ETE
ChainResidueDetails
AASN47

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gqg
ChainResidueDetails
AGLU95

site_idMCSA1
Number of Residues9
DetailsM-CSA 995
ChainResidueDetails
AASN75hydrogen bond acceptor
AVAL77steric role
AASN85hydrogen bond donor
AHIS88metal ligand
AHIS90metal ligand
AGLU95metal ligand
AHIS137metal ligand
AGLN139hydrogen bond acceptor, hydrogen bond donor
AMET149steric role

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PDB entries from 2024-11-06

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