PDBe 2pnr

X-ray diffraction
2.5Å resolution

Crystal Structure of the asymmetric Pdk3-l2 Complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial Chains: A, B, E, F
Molecule details ›
Chains: A, B, E, F
Length: 419 amino acids
Theoretical weight: 48.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q15120 (Residues: 9-406; Coverage: 98%)
Gene names: PDHK3, PDK3
Sequence domains:
Structure domains:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial Chains: C, G
Molecule details ›
Chains: C, G
Length: 128 amino acids
Theoretical weight: 14.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P10515 (Residues: 212-319; Coverage: 17%)
Gene names: DLAT, DLTA
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P41
Unit cell:
a: 96.155Å b: 96.155Å c: 222.984Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.176 0.229
Expression system: Escherichia coli BL21