Structure of PDB 2cog Chain A

Receptor sequence
>2cogA (length=358) Species: 9606 (Homo sapiens) [Search protein sequence]
VGTFKAKDLIVTPATILKEKPDPNLVFGTVFTDHMLTVEWSSEFGWEKPH
IKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR
SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPS
LGVKKPTKALLFVLLSPVGPYFNPVSLWANPKYVRAWKGGTGDCKMGGNY
GSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELA
TPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVRE
MFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGRE
ERDWTIVL
3D structure
PDB2cog Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K222
Catalytic site (residue number reindexed from 1) K195
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid 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 R119 K222 Y227 E257 T260 L286 G288 V289 T290 T333 R97 K195 Y200 E230 T233 L259 G261 V262 T263 T306
BS02 4MV A Y193 T260 T333 A334 Y171 T233 T306 A307
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0008483 transaminase activity
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0000082 G1/S transition of mitotic cell cycle
GO:0006629 lipid metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2cog, PDBe:2cog, PDBj:2cog
PDBsum2cog
PubMed16141215
UniProtP54687|BCAT1_HUMAN Branched-chain-amino-acid aminotransferase, cytosolic (Gene Name=BCAT1)

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