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Structure of PDB 1v2d Chain A Binding Site BS01

Receptor Information >1v2d Chain A (length=365) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] MRLHPRTEAAIFPRMSGLAQRLGAVNLGQGFPSNPPPPFLLEAVRRALGR QDQYAPPAGLPALREALAEEFAVEPESVVVTSGATEALYVLLQSLVGPGD EVVVLEPFFDVYLPDAFLAGAKARLVRLDLTPEGFRLDLSALEKALTPRT RALLLNTPMNPTGLVFGERELEAIARLARAHDLFLISDEVYDELYYGERP RRLREFAPERTFTVGSAGKRLEATGYRVGWIVGPKEFMPRLAGMRQWTSF SAPTPLQAGVAEALKLARREGFYEALREGYRRRRDLLAGGLRAMGLRVYV PEGTYFLMAELPGWDAFRLVEEARVALIPASAFYLEDPPKDLFRFAFCKT EEELHLALERLGRVV

Ligand information Ligand ID PLP InChI InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14) InChIKey NGVDGCNFYWLIFO-UHFFFAOYSA-N SMILES Software SMILES CACTVS 3.341 Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O OpenEye OEToolkits 1.5.0 Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O ACDLabs 10.04 O=P(O)(O)OCc1cnc(c(O)c1C=O)C Formula C8 H10 N O6 P Name PYRIDOXAL-5'-PHOSPHATE; VITAMIN B6 Phosphate ChEMBL CHEMBL82202 DrugBank DB00114 ZINC ZINC000001532514 PDB chain 1v2d Chain A Residue 510 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure 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] PDB 1v2d Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition Resolution 1.9 Å Binding residue (original residue number in PDB) G86 A87 T88 F112 N159 N163 D191 V193 Y194 S219 K222 R230 Binding residue (residue number reindexed from 1) G83 A84 T85 F109 N156 N160 D188 V190 Y191 S216 K219 R227 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) F112 A181 A183 K222 Catalytic site (residue number reindexed from 1) F109 A178 A180 K219 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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