Structure of PDB 1f8s Chain G Binding Site BS02

Receptor Information
>1f8s Chain G (length=482) Species: 8717 (Calloselasma rhodostoma) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMAGLSAAYVLAG
AGHQVTVLEASERPGGRVRTYRNEEAGWYANLGPMRLPEKHRIVREYIRK
FDLRLNEFSQENDNAWYFIKNIRKKVGEVKKDPGLLKYPVKPSEAGKSAG
QLYEESLGKVVEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLPTAMYRDIQDK
VHFNAQVIKIQQNDQKVTVVYETLSKETPSVTADYVIVCTTSRAVRLIKF
NPPLLPKKAHALRSVHYRSGTKIFLTCTTKFWEDDGIHGGKSTTDLPSRF
IYYPNHNFTNGVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDPLTASQGRIYF
AGEYTAQAHGWIDSTIKSGLRAARDVNLASEN
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 chain1f8s Chain G Residue 1545 [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]
PDB1f8s The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
Resolution2.0 Å
Binding residue
(original residue number in PDB)
L207 N208 E209 R322 I374
Binding residue
(residue number reindexed from 1)
L203 N204 E205 R318 I370
Annotation score1
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.
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1f8s, PDBe:1f8s, PDBj:1f8s
PDBsum1f8s
PubMed10944103
UniProtP81382|OXLA_CALRH L-amino-acid oxidase

[Back to BioLiP]