Structure of PDB 1v2f Chain A Binding Site BS03

Receptor Information

>1v2f Chain A (length=368) Species: 274 (Thermus thermophilus)

MRLHPRTEAAKESIFPRMSGLAQRLGAVNLGQGFPSNPPPPFLLEAVRRA
LGRQDQYAPPAGLPALREALAEEFAVEPESVVVTSGATEALYVLLQSLVG
PGDEVVVLEPFFDVYLPDAFLAGAKARLVRLDLTPEGFRLDLSALEKALT
PRTRALLLNTPMNPTGLVFGERELEAIARLARAHDLFLISDEVYDELYYG
ERPRRLREFAPERTFTVGSAGKRLEATGYRVGWIVGPKEFMPRLAGMRQW
TSFSAPTPLQAGVAEALKLARREGFYEALREGYRRRRDLLAGGLRAMGLR
VYVPEGTYFLMAELPGWDAFRLVEEARVALIPASAFYLEDPPKDLFRFAF
CKTEEELHLALERLGRVV

Ligand information

• Ligand ID: HCI
• InChI: InChI=1S/C9H10O2/c10-9(11)7-6-8-4-2-1-3-5-8/h1-5H,6-7H2,(H,10,11)
• InChIKey: XMIIGOLPHOKFCH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 12.01: O=C(O)CCc1ccccc1
  OpenEye OEToolkits 1.7.6: c1ccc(cc1)CCC(=O)O
  CACTVS 3.370: OC(=O)CCc1ccccc1
• Formula: C9 H10 O2
• Name: HYDROCINNAMIC ACID;
  3PP;
  3-PHENYLPROPIONIC ACID
• ChEMBL: CHEMBL851
• DrugBank: DB02024
• ZINC: ZINC000000154564
• PDB chain: 1v2f Chain B Residue 1520

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1v2f Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition
• Resolution: 2.35 Å
• Binding residue (original residue number in PDB): Y57 F253
• Binding residue (residue number reindexed from 1): Y57 F253
• Annotation score: 1

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

External links

• PDB: RCSB:1v2f, PDBe:1v2f, PDBj:1v2f
• PDBsum: 1v2f
• PubMed: 14761974
• UniProt: Q75WK2