3gkb

X-ray diffraction
1.8Å resolution

Crystal structure of a putative enoyl-CoA hydratase from Streptomyces avermitilis

Released:
Source organism: Streptomyces avermitilis
Entry authors: Bonanno JB, Freeman J, Bain KT, Chang S, Romero R, Wasserman S, Sauder JM, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative enoyl-CoA hydratase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 287 amino acids
Theoretical weight: 30.54 KDa
Source organism: Streptomyces avermitilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q82QL3 (Residues: 2-277; Coverage: 100%)
Gene names: SAVERM_492, echA1
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 58.461Å b: 87.502Å c: 154.447Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.206
Expression system: Escherichia coli