› 1iyv

Solution NMR

LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, 29 STRUCTURES

Released:
DOI: 10.2210/pdb1iyv/pdb
PDB entry 1iyv coloured by chain, ensemble of 29 models, front view.
PDB entry 1iyv coloured by chain, ensemble of 29 models, side view.
PDB entry 1iyv coloured by chain, ensemble of 29 models, top view.
Source organism: Azotobacter vinelandii
Primary publication:
Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
Berg A, Vervoort J, de Kok A
Eur J Biochem 244 352-60 (1997)
PMID: 9119000

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.17 KDa
Source organism: Azotobacter vinelandii
UniProt:
  • Canonical: P10802 (Residues: 2-79; Coverage: 12%)
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores

Quick links

Citations

4 review citations

Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
Perham RN. (2000)
3 more

1 mention without citation

TOUCHSTONE: an ab initio protein structure prediction method that uses threading-based tertiary restraints.
Kihara et al. (2001)