Structure of PDB 2jb3 Chain B

Receptor sequence

>2jb3B (length=477) Species: 37919 (Rhodococcus opacus)

DLIGKVKGSHSVVVLGGGPAGLCSAFELQKAGYKVTVLEARTRPGGRVWT
ARGGSEETDLSGETQKCTFSEGHFYNVGATRIPQSHITLDYCRELGVEIQ
GFGNQNANTFVNYQSDTSLSGQSVTYRAAKADTFGYMSELLKKATDQGAL
DQVLSREDKDALSEFLSDFGDLSDDGRYLGSSRRGYDSEPGAGLNFGTEK
KPFAMQEVIRSGIGRNFSFDFGYDQAMMMFTPVGGMDRIYYAFQDRIGTD
NIVFGAEVTSMKNVSEGVTVEYTAGGSKKSITADYAICTIPPHLVGRLQN
NLPGDVLTALKAAKPSSSGKLGIEYSRRWWETEDRIYGGASNTDKDISQI
MFPYDHYNSDRGVVVAYYSSGKRQEAFESLTHRQRLAKAIAEGSEIHGEK
YTRDISSSFSGSWRRTKYSESAWANWAGATPEYEKLLEPVDKIYFAGDHL
SNAIAWQHGALTSARDVVTHIHERVAQ

3D structure

• PDB: 2jb3 The Structure of a Bacterial L-Amino Acid Oxidase from Rhodococcus Opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation
• Chain: B
• Resolution: 1.85 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	B	G19 G21 P22 A23 E42 A43 R44 G49 R50 G81 A82 T83 R84 A259 V261 I293 Y371 W416 Y421 A425 G458 D459 A466 W467 Q468 A471	G16 G18 P19 A20 E39 A40 R41 G46 R47 G78 A79 T80 R81 A256 V258 I290 Y368 W413 Y418 A422 G447 D448 A455 W456 Q457 A460
BS02	BE2	B	R84 Y371 A466 W467	R81 Y368 A455 W456

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

External links

• PDB: RCSB:2jb3, PDBe:2jb3, PDBj:2jb3
• PDBsum: 2jb3
• PubMed: 17234209
• UniProt: Q8VPD4|OXLA_RHOOP L-amino acid oxidase