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2E1M

Crystal Structure of L-Glutamate Oxidase from Streptomyces sp. X-119-6

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
B0016491molecular_functionoxidoreductase activity
C0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 901
ChainResidue
AASN90
AARG93
ALYS99
CASP611

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AHIS220
BTYR421
BARG424

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 903
ChainResidue
ALEU306
AHIS307
CTHR622
CPRO623
ASER277
AARG283

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 801
ChainResidue
AGLY65
AGLY67
AILE68
AALA69
AGLU88
AALA89
AGLY95
AGLY96
AARG97
AILE98
AGLY121
AALA122
AMET123
AARG124
AGLN352
AARG353
AMET354
BILE405
BSER409
CTRP608
CTYR613
CGLU617
CGLY644
CGLU645
CALA652
CTRP653
CILE654
CALA657

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19531050, ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D
ChainResidueDetails
CGLU645
CTRP653
CILE654
AMET123
AARG124
AMET354

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:33764624, ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D
ChainResidueDetails
AALA89

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000269|PubMed:22197816, ECO:0000269|PubMed:33764624
ChainResidueDetails
AARG305

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
APRO126

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
AALA118

225158

PDB entries from 2024-09-18

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