Structure of PDB 2pnr Chain B

Receptor sequence
>2pnrB (length=341) Species: 9606 (Homo sapiens) [Search protein sequence]
KQIERYSRFSPSPLSIKQFLDFGRDNACEKTSYMFLRKELPVRLANTMRE
VNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDPQVLDNFLQVLI
KVRNRHNDVVPTMAQGVIEYKEKSTNIQYFLDRFYTNRISFRMLINQHTL
LFGGDTNPVHPKHIGSIDPTCNVADVVKDAYETAKMLCEQYYLVAPELEV
EEFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDYPAVKTLV
TLGKEDLSIKISDLGGGVPLRKIDRLFNYMGLPISRLYARYFQGDLKLYS
MEGVGTDAVIYLKALSSESFERLPVFNKSAWRHYKTADDWS
3D structure
PDB2pnr Crystal Structure of an Asymmetric complex of Pyruvate Dehydrogenase Kinase 3 with Lipoyl domain 2 and its Biological Implications
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H243 E247 K250 N251
Catalytic site (residue number reindexed from 1) H223 E227 K230 N231
Enzyme Commision number 2.7.11.2: [pyruvate dehydrogenase (acetyl-transferring)] kinase.
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 RED B Q31 F35 F48 Q18 F22 F35
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004740 pyruvate dehydrogenase (acetyl-transferring) kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0010510 regulation of acetyl-CoA biosynthetic process from pyruvate
GO:0010906 regulation of glucose metabolic process
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0035357 peroxisome proliferator activated receptor signaling pathway
GO:0071333 cellular response to glucose stimulus
GO:0071398 cellular response to fatty acid
GO:0097411 hypoxia-inducible factor-1alpha signaling pathway
GO:2000377 regulation of reactive oxygen species metabolic process
Cellular Component
GO:0005730 nucleolus
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:2pnr, PDBe:2pnr, PDBj:2pnr
PDBsum2pnr
PubMed17532006
UniProtQ15120|PDK3_HUMAN [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (Gene Name=PDK3)

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