› 3gqt

X-ray diffraction
1.99Å resolution

Crystal structure of glutaryl-CoA dehydrogenase from Burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methylamine

Released:
DOI: 10.2210/pdb3gqt/pdb
PDB entry 3gqt coloured by chain, front view.
PDB entry 3gqt coloured by chain, side view.
PDB entry 3gqt coloured by chain, top view.
Source organism: Burkholderia pseudomallei 1710b
Primary publication:
Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening.
Begley DW, Davies DR, Hartley RC, Hewitt SN, Rychel AL, Myler PJ, Van Voorhis WC, Staker BL, Stewart LJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1060-9 (2011)
PMID: 21904051

Function and Biology Details

Reaction catalysed: 
(1a) glutaryl-CoA + electron-transfer flavoprotein = (E)-glutaconyl-CoA + reduced electron-transfer flavoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glutaryl-CoA dehydrogenase (ETF) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 399 amino acids
Theoretical weight: 43.47 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JP94 (Residues: 1-395; Coverage: 100%)
Gene name: BURPS1710b_3237
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand UFO 3 x UFO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 97.418Å b: 106.374Å c: 144.774Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.238
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening.
Begley et al. (2011)