Structure of PDB 3exh Chain E

Receptor sequence
>3exhE (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
MFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKA
DQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRG
LSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIA
LACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRER
AAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQ
TYSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEP
PLEELGYHIYSSDPPFEVRGANQWIKFKSVS
3D structure
PDB3exh Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
ChainE
Resolution2.444 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q51 G136
Catalytic site (residue number reindexed from 1) Q52 G137
Enzyme Commision number 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring).
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 MN E D167 N196 D168 N197
BS02 TPP E Y89 R90 V138 G166 D167 G168 N196 Y90 R91 V139 G167 D168 G169 N197
Gene Ontology
Molecular Function
GO:0004738 pyruvate dehydrogenase activity
GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
GO:0034604 pyruvate dehydrogenase (NAD+) activity
GO:0046872 metal ion binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006086 acetyl-CoA biosynthetic process from pyruvate
GO:0006090 pyruvate metabolic process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005634 nucleus
GO:0005730 nucleolus
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0043231 intracellular membrane-bounded organelle
GO:0045254 pyruvate dehydrogenase complex
GO:1902494 catalytic complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:3exh, PDBe:3exh, PDBj:3exh
PDBsum3exh
PubMed19081061
UniProtP08559|ODPA_HUMAN Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (Gene Name=PDHA1)

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