› 2j9f

X-ray diffraction
1.88Å resolution

Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase E1b

Released:
DOI: 10.2210/pdb2j9f/pdb
PDB entry 2j9f coloured by chain, front view.
PDB entry 2j9f coloured by chain, side view.
PDB entry 2j9f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism.
Li J, Machius M, Chuang JL, Wynn RM, Chuang DT
J Biol Chem 282 11904-13 (2007)
PMID: 17329260

Function and Biology Details

Reaction catalysed: 
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146300 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial Chains: A, C
Molecule details ›
Chains: A, C
Length: 400 amino acids
Theoretical weight: 45.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P12694 (Residues: 46-445; Coverage: 90%)
Gene name: BCKDHA
Sequence domains: Dehydrogenase E1 component
Structure domains: Rossmann fold
2-oxoisovalerate dehydrogenase subunit beta, mitochondrial Chains: B, D
Molecule details ›
Chains: B, D
Length: 350 amino acids
Theoretical weight: 38.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P21953 (Residues: 51-392; Coverage: 87%)
Gene name: BCKDHB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand THV 2 x THV
3 bound ligands:
Ligand MN 2 x MN
Ligand K 4 x K
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P3221
Unit cell:
a: 145.342Å b: 145.342Å c: 138.05Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.17 0.2
Expression system: Escherichia coli BL21

Quick links

Citations

8 citation in other articles

Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
Kato et al. (2008)
7 more

1 mention without citation

Maple syrup urine disease in Cypriot families: identification of three novel mutations and biochemical characterization of the p.Thr211Met mutation in the E1alpha subunit.
Georgiou et al. (2009)