Structure of PDB 2ozl Chain A

Receptor sequence
>2ozlA (length=362) Species: 9606 (Homo sapiens) [Search protein sequence]
SFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKA
DQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRG
LSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIA
LACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYG
MGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKG
PILMELQTYRYHGHEMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSN
LASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVR
GANQWIKFKSVS
3D structure
PDB2ozl Phosphorylation of Serine 264 Impedes Active Site Accessibility in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex
ChainA
Resolution1.9 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 E264 Y272
Catalytic site (residue number reindexed from 1) Q52 G137 R260 H264 E265 Y273
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 A D167 N196 Y198 D168 N197 Y199
BS02 TPP A Y89 R90 V138 G166 D167 G168 A169 N196 Y198 G199 H263 Y90 R91 V139 G167 D168 G169 A170 N197 Y199 G200 H264 MOAD: Kd=0.92uM
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:2ozl, PDBe:2ozl, PDBj:2ozl
PDBsum2ozl
PubMed17474719
UniProtP08559|ODPA_HUMAN Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (Gene Name=PDHA1)

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