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Entry Information
Entry status
(1)
Experimental methods
(1)
X-ray diffraction
(5)
Authors
(9)
Chuang DT
(4)
Chuang JL
(4)
Kato M
(4)
Tso SC
(3)
Wynn RM
(3)
Devedjiev Y
(1)
Li J
(1)
Steussy CN
(1)
Vassylyev DG
(1)
Homo / hetero assembly
(1)
hetero
(5)
Assembly composition
(1)
protein/protein complex
(5)
Assembly polymer count
(2)
tetramer
(4)
trimer
(1)
Resolution distribution
2.0 - 2.5
(2)
2.5 - 3
(3)
Release year distribution
2000 - 2005
(3)
2005 - 2010
(5)
Journal
(3)
EMBO J
(3)
J Mol Biol
(1)
Structure
(1)
Macromolecules
Organism superkingdom
(1)
Eukaryota
(5)
Organism name
(1)
Homo sapiens
(5)
Molecule name
(2)
Pyruvate dehydrogenase kinase isoform 3
(5)
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial
(5)
Molecule type
(1)
Protein
(5)
Gene names
(2)
PDHK3
(5)
PDK3
(5)
Interacting Molecules
(1)
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
(5)
Interacting ligands
(7)
RED : DIHYDROLIPOIC ACID
(5)
K : POTASSIUM ION
(4)
MG : MAGNESIUM ION
(2)
ADP : ADENOSINE-5'-DIPHOSPHATE
(1)
ATP : ADENOSINE-5'-TRIPHOSPHATE
(1)
GOL : GLYCEROL
(1)
RDC : RADICICOL
(1)
Function and Biology
EC number / name
(1)
2.7.11.2 : [Pyruvate dehydrogenase (acetyl-transferring)] kinase
(5)
Biological function
(8)
ATP binding
(5)
kinase activity
(5)
nucleotide binding
(5)
protein binding
(5)
protein kinase activity
(5)
protein serine/threonine kinase activity
(5)
pyruvate dehydrogenase (acetyl-transferring) kinase activity
(5)
transferase activity
(5)
Biological process
(8)
cellular response to fatty acid
(5)
cellular response to glucose stimulus
(5)
hypoxia-inducible factor-1alpha signaling pathway
(5)
peptidyl-serine phosphorylation
(5)
peroxisome proliferator activated receptor signaling pathway
(5)
regulation of acetyl-CoA biosynthetic process from pyruvate
(5)
regulation of glucose metabolic process
(5)
regulation of reactive oxygen species metabolic process
(5)
Biological cell component
(3)
mitochondrial matrix
(5)
mitochondrion
(5)
nucleolus
(5)
Sequence and Structure classification
SCOP fold
(2)
ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
(5)
Bromodomain-like
(5)
SCOP family
(2)
alpha-ketoacid dehydrogenase kinase, C-terminal domain
(5)
alpha-ketoacid dehydrogenase kinase, N-terminal domain
(5)
CATH class
(2)
Alpha Beta
(5)
Mainly Alpha
(5)
CATH topology
(2)
Butyryl-CoA Dehydrogenase, subunit A; domain 3
(5)
Heat Shock Protein 90
(5)
Pfam accession / name
(2)
PF02518 : HATPase_c
(5)
PF10436 : BCDHK_Adom3
(5)
Experimental Information
Diffraction protocol
(1)
Single wavelength
(5)
Diffraction radiation source type
(2)
Synchrotron
(4)
Rotating anode
(1)
Diffraction source
(4)
APS BEAMLINE 19-ID
(2)
APS BEAMLINE 17-ID
(1)
APS BEAMLINE 19-BM
(1)
RIGAKU RU200
(1)
Synchrotron site
(1)
APS
(4)
Diffraction detector type
(2)
CCD
(4)
Image plate
(1)
Refinement software
(2)
REFMAC
(4)
CNS
(1)
Representative Structures
Representative Structures
Entries
Macromolecules
Compounds
Protein families
Entries 1 to 5 of 5
Select all entries on this page
Crystal structure of the PDK3-L2 complex
Kato M, Chuang JL, Wynn RM, Chuang DT
EMBO J
(2005)
[PMID: 15861126 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial and Dihydrolipoyllysine-residue acetyltransferase component of pyruvate...
(Preferred)
show full assembly name search this complex
show full assembly name search this complex
PDBe complex ID:
PDB-CPX-145328 (Preferred)
search this ID
Pyruvate dehydrogenase kinase isoform 3 in complex with antitumor drug radicicol
Kato M, Li J, Chuang JL, Chuang DT
Structure
(2007)
[PMID: 17683942 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial and Dihydrolipoyllysine-residue acetyltransferase component of pyruvate...
(Preferred)
show full assembly name search this complex
show full assembly name search this complex
PDBe complex ID:
PDB-CPX-145328 (Preferred)
search this ID
Crystal structure of the PDK3-L2 complex
Kato M, Chuang JL, Wynn RM, Chuang DT
EMBO J
(2005)
[PMID: 15861126 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial and Dihydrolipoyllysine-residue acetyltransferase component of pyruvate...
(Preferred)
show full assembly name search this complex
show full assembly name search this complex
PDBe complex ID:
PDB-CPX-145328 (Preferred)
search this ID
Crystal structure of the PDK3-L2 complex
Kato M, Chuang JL, Wynn RM, Chuang DT
EMBO J
(2005)
[PMID: 15861126 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial and Dihydrolipoyllysine-residue acetyltransferase component of pyruvate...
(Preferred)
show full assembly name search this complex
show full assembly name search this complex
PDBe complex ID:
PDB-CPX-145328 (Preferred)
search this ID
Crystal Structure of the asymmetric Pdk3-l2 Complex
Vassylyev DG, Steussy CN, Devedjiev Y
J Mol Biol
(2007)
[PMID: 17532006 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial and Dihydrolipoyllysine-residue acetyltransferase component of pyruvate...
(Preferred)
show full assembly name search this complex
show full assembly name search this complex
PDBe complex ID:
PDB-CPX-145327 (Preferred)
search this ID
Entries 1 to 5 of 5