Structure of PDB 3exf Chain C

Receptor sequence
>3exfC (length=363) Species: 9606 (Homo sapiens) [Search protein sequence]
HMFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELK
ADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTR
GLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGI
ALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRY
GMGTAVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGK
GPILMELQTYRYHGHSMSDPGVAYRTREEIQEVRSKSDPIMLLKDRMVNS
NLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEV
RGANQWIKFKSVS
3D structure
PDB3exf Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
ChainC
Resolution2.998 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 R259 H263 S264 Y272
Catalytic site (residue number reindexed from 1) Q53 G138 R261 H265 S266 Y274
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 MG C D167 N196 Y198 D169 N198 Y200
BS02 TPP C Y89 R90 V138 G166 D167 G168 Y198 G199 M200 Y91 R92 V140 G168 D169 G170 Y200 G201 M202
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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Biological Process
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Cellular Component
External links
PDB RCSB:3exf, PDBe:3exf, PDBj:3exf
PDBsum3exf
PubMed19081061
UniProtP08559|ODPA_HUMAN Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (Gene Name=PDHA1)

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