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BioLiP

Structure of PDB 1f8s Chain C

Receptor sequence
>1f8sC (length=482) Species: 8717 (Calloselasma rhodostoma) [Search protein sequence]
NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMAGLSAAYVLAG
AGHQVTVLEASERPGGRVRTYRNEEAGWYANLGPMRLPEKHRIVREYIRK
FDLRLNEFSQENDNAWYFIKNIRKKVGEVKKDPGLLKYPVKPSEAGKSAG
QLYEESLGKVVEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLPTAMYRDIQDK
VHFNAQVIKIQQNDQKVTVVYETLSKETPSVTADYVIVCTTSRAVRLIKF
NPPLLPKKAHALRSVHYRSGTKIFLTCTTKFWEDDGIHGGKSTTDLPSRF
IYYPNHNFTNGVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDPLTASQGRIYF
AGEYTAQAHGWIDSTIKSGLRAARDVNLASEN
3D structure
PDB1f8s The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
ChainC
Resolution2.0 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) P88 H219 K322
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
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: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:1f8s, PDBe:1f8s, PDBj:1f8s
PDBsum1f8s
PubMed10944103
UniProtP81382|OXLA_CALRH L-amino-acid oxidase

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