PDBe 3crl

X-ray diffraction
2.61Å resolution

Crystal structure of the PDHK2-L2 complex.

Released:

Function and Biology Details

Reactions catalysed:
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 407 amino acids
Theoretical weight: 46.16 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q64536 (Residues: 1-407; Coverage: 100%)
Gene name: Pdk2
Sequence domains:
Structure domains:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial Chains: C, D
Molecule details ›
Chains: C, D
Length: 87 amino acids
Theoretical weight: 9.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10515 (Residues: 214-300; Coverage: 13%)
Gene names: DLAT, DLTA
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 71.413Å b: 121.63Å c: 71.452Å
α: 90° β: 97.29° γ: 90°
R-values:
R R work R free
0.223 0.22 0.274
Expression system: Escherichia coli BL21(DE3)