Structure of PDB 5ts5 Chain D

Receptor sequence
>5ts5D (length=479) Species: 8725 (Bothrops atrox) [Search protein sequence]
PLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANA
GHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIRKF
DLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQ
LYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGD
LLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKV
HLNARVIKIQQDVKEVTVTYQTSEKETLSVTADYVIVCTTSRAARRIKFE
PPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFI
YYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPK
EEIQAICRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFA
GEYTAQAHGWIDSTIKSGLRAARDVNRAS
3D structure
PDB5ts5 Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P92 H223 K326
Catalytic site (residue number reindexed from 1) P87 H218 K321
Enzyme Commision number 1.4.3.2: L-amino-acid oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0001716 L-amino-acid oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0090729 toxin activity
GO:0106329 L-phenylalaine oxidase activity
Biological Process
GO:0006915 apoptotic process
GO:0009063 amino acid catabolic process
GO:0031640 killing of cells of another organism
GO:0042742 defense response to bacterium
GO:0044478 envenomation resulting in positive regulation of platelet aggregation in another organism
GO:0044532 modulation of apoptotic process in another organism
GO:0050829 defense response to Gram-negative bacterium
GO:0050830 defense response to Gram-positive bacterium
GO:0090330 regulation of platelet aggregation
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ts5, PDBe:5ts5, PDBj:5ts5
PDBsum5ts5
PubMed28137621
UniProtP0CC17|OXLA_BOTAT L-amino-acid oxidase

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