Structure of PDB 1v2e Chain A

Receptor sequence
>1v2eA (length=368) Species: 274 (Thermus thermophilus) [Search protein sequence]
MRLHPRTEAAKESIFPRMSGLAQRLGAVNLGQGFPSNPPPPFLLEAVRRA
LGRQDQYAPPAGLPALREALAEEFAVEPESVVVTSGATEALYVLLQSLVG
PGDEVVVLEPFFDVYLPDAFLAGAKARLVRLDLTPEGFRLDLSALEKALT
PRTRALLLNTPMNPTGLVFGERELEAIARLARAHDLFLISDEVYDELYYG
ERPRRLREFAPERTFTVGSAGKRLEATGYRVGWIVGPKEFMPRLAGMRQW
TSFSAPTPLQAGVAEALKLARREGFYEALREGYRRRRDLLAGGLRAMGLR
VYVPEGTYFLMAELPGWDAFRLVEEARVALIPASAFYLEDPPKDLFRFAF
CKTEEELHLALERLGRVV
3D structure
PDB1v2e Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLP A G86 A87 T88 F112 D191 V193 Y194 S219 K222 R230 G86 A87 T88 F112 D191 V193 Y194 S219 K222 R230
BS02 KMT A F15 Q32 G33 F112 K222 F309 R347 F15 Q32 G33 F112 K222 F309 R347
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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Cellular Component
External links
PDB RCSB:1v2e, PDBe:1v2e, PDBj:1v2e
PDBsum1v2e
PubMed14761974
UniProtQ75WK2

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