Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

pdhC (P11961) - Overview - Molecular Target Synopsis

Protein


pdhC, Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Enzyme Classification 2.3.1.12
UniProt P11961

Also Known as ODP2_GEOSE, pdhC

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). Forms a 60-polypeptide structural core with icosahedral symmetry.

3DVA
SNAPSHOTS OF CATALYSIS IN THE E1 SUBUNIT OF THE PYRUVATE DEHYDROGENASE MULTI-ENZYME COMPLEX
RCSB/PDB
Inspect Structure
See all 3D Structures for pdhC

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
428P11961-1

Gene Copy Number Variation


In COSMIC - Cell Lines Project pdhC has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For pdhC there are:
15 structures (24 chains) solved
0 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


pdhC has been screened with compounds ( bioactivities). (see details)