Structure of PDB 3d2r Chain B

Receptor sequence
>3d2rB (length=362) Species: 9606 (Homo sapiens) [Search protein sequence]
VPREVEHFSRYSPSPLSMKQLLDFGSENACERTSFAFLRQELPVRLANIL
KEIDILPTQLVNTSSVQLVKSWYIQSLMDLVEFHEKSPDDQKALSDFVDT
LIKVRNRHHNVVPTMAQGIIEYKACTVDPVTNQNLQYFLDRFYMNRISTR
MLMNQHILIFSDSQTGNPSHIGSIDPNCDVVAVVQDAFECSRMLCDQYYL
SSPELKLTQVNGKFPDQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENQ
PSLTPIEVIVVLGKEDLTIKISDRGGGVPLRIIDRLFSYTYSTAPTPPLA
GFGYGLPISRLYAKYFQGDLNLYSLSGYGTDAIIYLKALSSESIEKLPVF
NKSAFKHYDWCI
3D structure
PDB3d2r Pyruvate Dehydrogenase Kinase-4 Structures Reveal a Metastable Open Conformation Fostering Robust Core-free Basal Activity.
ChainB
Resolution2.03 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) H250 E254 K257 N258
Catalytic site (residue number reindexed from 1) H230 E234 K237 N238
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 ADP B N258 A262 V298 L306 S312 T313 A328 G329 G331 G333 L334 N238 A242 V278 L286 S292 T293 A300 G301 G303 G305 L306 MOAD: Kd=3.3uM
Gene Ontology
Molecular Function
GO:0004672 protein 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:0006885 regulation of pH
GO:0008286 insulin receptor signaling pathway
GO:0009267 cellular response to starvation
GO:0010510 regulation of acetyl-CoA biosynthetic process from pyruvate
GO:0010565 regulation of cellular ketone metabolic process
GO:0010906 regulation of glucose metabolic process
GO:0016310 phosphorylation
GO:0042304 regulation of fatty acid biosynthetic process
GO:0042593 glucose homeostasis
GO:0042594 response to starvation
GO:0045124 regulation of bone resorption
GO:0046320 regulation of fatty acid oxidation
GO:0071398 cellular response to fatty acid
GO:0072593 reactive oxygen species metabolic process
GO:2000811 negative regulation of anoikis
Cellular Component
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:3d2r, PDBe:3d2r, PDBj:3d2r
PDBsum3d2r
PubMed18658136
UniProtQ16654|PDK4_HUMAN [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (Gene Name=PDK4)

[Back to BioLiP]