Structure of PDB 2jb3 Chain A Binding Site BS02

Receptor Information
>2jb3 Chain A (length=478) Species: 37919 (Rhodococcus opacus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLIGKVKGSHSVVVLGGGPAGLCSAFELQKAGYKVTVLEARTRPGGRVWT
ARGGSEETDLSGETQKCTFSEGHFYNVGATRIPQSHITLDYCRELGVEIQ
GFGNQNANTFVNYQSDTSLSGQSVTYRAAKADTFGYMSELLKKATDQGAL
DQVLSREDKDALSEFLSDFGDLSDDGRYLGSSRRGYDSEPGAGLNFGTEK
KPFAMQEVIRSGIGRNFSFDFGYDQAMMMFTPVGGMDRIYYAFQDRIGTD
NIVFGAEVTSMKNVSEGVTVEYTAGGSKKSITADYAICTIPPHLVGRLQN
NLPGDVLTALKAAKPSSSGKLGIEYSRRWWETEDRIYGGASNTDKDISQI
MFPYDHYNSDRGVVVAYYSSGKRQEAFESLTHRQRLAKAIAEGSEIHGEK
YTRDISSSFSGSWRRTKYSESAWANWAGSATPEYEKLLEPVDKIYFAGDH
LSNAIAWQHGALTSARDVVTHIHERVAQ
Ligand information
Ligand IDBE2
InChIInChI=1S/C7H7NO2/c8-6-4-2-1-3-5(6)7(9)10/h1-4H,8H2,(H,9,10)
InChIKeyRWZYAGGXGHYGMB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ccccc1C(O)=O
ACDLabs 10.04O=C(O)c1ccccc1N
OpenEye OEToolkits 1.5.0c1ccc(c(c1)C(=O)O)N
FormulaC7 H7 N O2
Name2-AMINOBENZOIC ACID
ChEMBLCHEMBL14173
DrugBankDB04166
ZINCZINC000000047985
PDB chain2jb3 Chain A Residue 1490 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2jb3 The Structure of a Bacterial L-Amino Acid Oxidase from Rhodococcus Opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation
Resolution1.85 Å
Binding residue
(original residue number in PDB)		R84 Y371 A466 W467
Binding residue
(residue number reindexed from 1)		R81 Y368 A456 W457
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R218 K323
Catalytic site (residue number reindexed from 1) R215 K320
Enzyme Commision number 1.4.3.2: L-amino-acid oxidase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0001716 L-amino-acid oxidase activity
GO:0016491 oxidoreductase activity
GO:0050025 L-glutamate oxidase activity
GO:0050029 L-lysine oxidase activity
GO:0106329 L-phenylalaine oxidase activity
Biological Process
GO:0009063 amino acid catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2jb3, PDBe:2jb3, PDBj:2jb3
PDBsum2jb3
PubMed17234209
UniProtQ8VPD4|OXLA_RHOOP L-amino acid oxidase

[Back to BioLiP]