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

7E0C

Structure of L-glutamate oxidase R305E mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001716molecular_functionL-amino-acid oxidase activity
A0005576cellular_componentextracellular region
A0009063biological_processamino acid catabolic process
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues37
Detailsbinding site for residue FAD A 900
ChainResidue
AGLY65
AILE98
AGLY121
AALA122
AMET123
AARG124
AARG317
AGLN352
AARG353
AMET354
AILE405
AGLY67
ASER409
ATRP608
ATYR613
AGLU617
AGLY644
AGLU645
AALA652
ATRP653
AILE654
AALA657
AILE68
AHOH1005
AHOH1007
AHOH1021
AHOH1026
AHOH1030
AHOH1044
AHOH1063
AHOH1068
AALA69
AGLU88
AALA89
AGLY95
AGLY96
AARG97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:19531050, ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D
ChainResidueDetails
AALA69
AGLU88
AARG97
AMET123
AARG124
AMET354
ASER409
AGLU645
ATRP653
AILE654

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
AGLU305

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon