PDBe 1hzd

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF HUMAN AUH PROTEIN, AN RNA-BINDING HOMOLOGUE OF ENOYL-COA HYDRATASE

Released:

Function and Biology Details

Reaction catalysed:
(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylglutaconyl-CoA hydratase, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 272 amino acids
Theoretical weight: 29.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13825 (Residues: 68-339; Coverage: 80%)
Gene name: AUH
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P21
Unit cell:
a: 79.13Å b: 132.07Å c: 80.04Å
α: 90° β: 108.14° γ: 90°
R-values:
R R work R free
0.212 0.207 0.253
Expression system: Escherichia coli BL21(DE3)