Structure of PDB 1tdo Chain A

Receptor sequence
>1tdoA (length=484) Species: 8714 (Gloydius halys) [Search protein sequence]
DRNPLEECFRETDYEEFLEIARNGLKATSNPKHVVVVGAGMSGLSAAYVL
SGAGHQVTVLEASERAGGRVRTYRNDKEDWYANLGPMRLPEKHRIVREYI
RKFGLQLNEFSQENDNAWYFIKNIRKRVGEVKKDPGVLKYPVKPSEEGKS
AGQLYEESLGKVVEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDM
IGDLMNEDSGYYVSFPESLRHDDIFAYEKRFDEIVGGMDKLPTSMYRAIE
EKVHLNAQVIKIQKNAEKVTVVYQTPAKEMASVTADYVIVCTTSRATRRI
KFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDEGIHGGKSTTDLPS
RFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQ
LPREEIQTFCYPSMIQKWSLDKYAMGGITTFTPYQFQHFSESLTASVDRI
YFAGEHTAEAHGWIDSTIKSGLRAARDVNRASEQ
3D structure
PDB1tdo Structures of L-amino acid oxidase in complexes with substrates and substrate analogue
ChainA
Resolution3.0 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) P90 H221 K324
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:0090729 toxin activity
Biological Process
GO:0006915 apoptotic process
GO:0009063 amino acid catabolic process
GO:0031640 killing of cells of another organism
GO:0035821 modulation of process of another organism
GO:0042742 defense response to bacterium
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:1tdo, PDBe:1tdo, PDBj:1tdo
PDBsum1tdo
PubMed
UniProtQ6STF1|OXLA_GLOHA L-amino-acid oxidase

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