Structure of PDB 1kta Chain B

Receptor sequence
>1ktaB (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
ASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQ
PRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRM
LRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNE
PSLGVSQPRRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGN
YKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHE
DGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRAL
EEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELK
EIQYGIRAHEWMFPV
3D structure
PDB1kta Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K702
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 KIV B Y570 V655 Y70 V155
BS02 PMP B R599 R692 K702 Y707 E737 T740 M741 N742 L766 G768 V769 V770 T813 R99 R192 K202 Y207 E237 T240 M241 N242 L266 G268 V269 V270 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1kta, PDBe:1kta, PDBj:1kta
PDBsum1kta
PubMed12269802
UniProtO15382|BCAT2_HUMAN Branched-chain-amino-acid aminotransferase, mitochondrial (Gene Name=BCAT2)

[Back to BioLiP]