Structure of PDB 2abj Chain D

Receptor sequence
>2abjD (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
VVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEK
PHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPAFIGTE
PSLGVKKPTKALLFVLLSPVGPFNPVSLWANPKYVRAWKGGTGDCKMGGN
YGSSLFAQCEDVDNGCQQVLWLYGRDHQITEVGTMNLFLYWINEDGEEEL
ATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVR
EMFSSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGR
EESDWTIVL
3D structure
PDB2abj The design and synthesis of human branched-chain amino acid aminotransferase inhibitors for treatment of neurodegenerative diseases.
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K220
Catalytic site (residue number reindexed from 1) K196
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 CBC D F47 F93 Y159 K220 Q242 T258 M259 G330 A332 C333 F29 F75 Y141 K196 Q218 T234 M235 G306 A308 C309 MOAD: ic50=0.8uM
BindingDB: IC50=230nM
BS02 PLP D R117 K220 Y225 E255 T258 M259 N260 L284 G286 V287 T288 T331 R99 K196 Y201 E231 T234 M235 N236 L260 G262 V263 T264 T307
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:2abj, PDBe:2abj, PDBj:2abj
PDBsum2abj
PubMed16143519
UniProtP54687|BCAT1_HUMAN Branched-chain-amino-acid aminotransferase, cytosolic (Gene Name=BCAT1)

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