Structure of PDB 1v2f Chain A Binding Site BS02

Receptor Information
>1v2f Chain A (length=368) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRLHPRTEAAKESIFPRMSGLAQRLGAVNLGQGFPSNPPPPFLLEAVRRA
LGRQDQYAPPAGLPALREALAEEFAVEPESVVVTSGATEALYVLLQSLVG
PGDEVVVLEPFFDVYLPDAFLAGAKARLVRLDLTPEGFRLDLSALEKALT
PRTRALLLNTPMNPTGLVFGERELEAIARLARAHDLFLISDEVYDELYYG
ERPRRLREFAPERTFTVGSAGKRLEATGYRVGWIVGPKEFMPRLAGMRQW
TSFSAPTPLQAGVAEALKLARREGFYEALREGYRRRRDLLAGGLRAMGLR
VYVPEGTYFLMAELPGWDAFRLVEEARVALIPASAFYLEDPPKDLFRFAF
CKTEEELHLALERLGRVV
Ligand information
Ligand IDHCI
InChIInChI=1S/C9H10O2/c10-9(11)7-6-8-4-2-1-3-5-8/h1-5H,6-7H2,(H,10,11)
InChIKeyXMIIGOLPHOKFCH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)CCc1ccccc1
OpenEye OEToolkits 1.7.6c1ccc(cc1)CCC(=O)O
CACTVS 3.370OC(=O)CCc1ccccc1
FormulaC9 H10 O2
NameHYDROCINNAMIC ACID;
3PP;
3-PHENYLPROPIONIC ACID
ChEMBLCHEMBL851
DrugBankDB02024
ZINCZINC000000154564
PDB chain1v2f Chain A Residue 520 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1v2f Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition
Resolution2.35 Å
Binding residue
(original residue number in PDB)		F15 Q32 G33 F112 R347
Binding residue
(residue number reindexed from 1)		F15 Q32 G33 F112 R347
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F112 A181 A183 K222
Catalytic site (residue number reindexed from 1) F112 A181 A183 K222
Enzyme Commision number 2.6.1.15: glutamine--pyruvate transaminase.
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1v2f, PDBe:1v2f, PDBj:1v2f
PDBsum1v2f
PubMed14761974
UniProtQ75WK2

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