Structure of PDB 2abj Chain D Binding Site BS02

Receptor Information
>2abj Chain D (length=359) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEK
PHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPAFIGTE
PSLGVKKPTKALLFVLLSPVGPFNPVSLWANPKYVRAWKGGTGDCKMGGN
YGSSLFAQCEDVDNGCQQVLWLYGRDHQITEVGTMNLFLYWINEDGEEEL
ATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVR
EMFSSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGR
EESDWTIVL
Ligand information
Ligand IDPLP
InChIInChI=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)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain2abj Chain D Residue 420 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2abj The design and synthesis of human branched-chain amino acid aminotransferase inhibitors for treatment of neurodegenerative diseases.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		R117 K220 Y225 E255 T258 M259 N260 L284 G286 V287 T288 T331
Binding residue
(residue number reindexed from 1)		R99 K196 Y201 E231 T234 M235 N236 L260 G262 V263 T264 T307
Annotation score1
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.
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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