Structure of PDB 2abj Chain A

Receptor sequence
>2abjA (length=366) Species: 9606 (Homo sapiens) [Search protein sequence]
VVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEK
PHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPAFIGTE
PSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGD
CKMGGNYGSSLFAQCEDVDNGCQQVLWLYGRDHQITEVGTMNLFLYWINE
DGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTAL
EGNRVREMFSSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLT
DIQYGREESDWTIVLS
3D structure
PDB2abj The design and synthesis of human branched-chain amino acid aminotransferase inhibitors for treatment of neurodegenerative diseases.
ChainA
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) K202
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 A F47 F93 Y159 Y191 K220 Q242 T258 M259 G330 A332 C333 F29 F75 Y141 Y173 K202 Q224 T240 M241 G312 A314 C315 MOAD: ic50=0.8uM
BindingDB: IC50=230nM
BS02 PLP A R117 R210 K220 Y225 E255 T258 M259 N260 L284 G286 V287 T288 T331 R99 R192 K202 Y207 E237 T240 M241 N242 L266 G268 V269 T270 T313
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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