PDBe 3rnm

X-ray diffraction
2.4Å resolution

The crystal structure of the subunit binding of human dihydrolipoamide transacylase (E2b) bound to human dihydrolipoamide dehydrogenase (E3)

Released:

Function and Biology Details

Reactions catalysed:
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH
2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydrolipoyl dehydrogenase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 495 amino acids
Theoretical weight: 52.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09622 (Residues: 36-509; Coverage: 93%)
  • Best match: P09622-2 (Residues: 1-410)
Gene names: DLD, GCSL, LAD, PHE3
Sequence domains:
Structure domains:
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Chains: E, F
Molecule details ›
Chains: E, F
Length: 58 amino acids
Theoretical weight: 6.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11182 (Residues: 165-213; Coverage: 10%)
Gene names: BCATE2, DBT
Sequence domains: e3 binding domain
Structure domains: E3-binding domain

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 84.136Å b: 112.308Å c: 122.545Å
α: 90° β: 91.4° γ: 90°
R-values:
R R work R free
0.184 0.181 0.24
Expression system: Escherichia coli