3el6

X-ray diffraction
1.85Å resolution

Crystal Structure of the Erythromycin Dehydratase

Released:
Source organism: Saccharopolyspora erythraea
Primary publication:
Crystal structure of the erythromycin polyketide synthase dehydratase.
J Mol Biol 384 941-53 (2008)
PMID: 18952099

Function and Biology Details

Reaction catalysed:
Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO(2) + H(2)O + 6 NADP(+)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-169840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-deoxyerythronolide-B synthase EryA2, modules 3 and 4 Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 32.72 KDa
Source organism: Saccharopolyspora erythraea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03132 (Residues: 2362-2653; Coverage: 8%)
Gene name: eryA
Sequence domains:
Structure domains: Polyketide synthase dehydratase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P43212
Unit cell:
a: 66.997Å b: 66.997Å c: 186.238Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.227
Expression system: Escherichia coli