Structure of PDB 1ekv Chain A

Receptor sequence
>1ekvA (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
ASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQ
PRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRM
LRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNE
PSLGVSQPRRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGN
YKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHE
DGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRAL
EEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELK
EIQYGIRAHEWMFPV
3D structure
PDB1ekv The structure of human mitochondrial branched-chain aminotransferase.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K202
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 PLP A R99 R192 Y207 E237 T240 M241 N242 G268 V269 V270 G312 T313 R99 R192 Y207 E237 T240 M241 N242 G268 V269 V270 G312 T313
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0005515 protein binding
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:0006549 isoleucine metabolic process
GO:0006550 isoleucine catabolic process
GO:0006551 L-leucine metabolic process
GO:0006573 valine metabolic process
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:0009083 branched-chain amino acid catabolic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0010817 regulation of hormone levels
GO:1990830 cellular response to leukemia inhibitory factor
Cellular Component
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ekv, PDBe:1ekv, PDBj:1ekv
PDBsum1ekv
PubMed11264579
UniProtO15382|BCAT2_HUMAN Branched-chain-amino-acid aminotransferase, mitochondrial (Gene Name=BCAT2)

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