4izb

X-ray diffraction
1.5Å resolution

Crystal structure of DmdD, a crotonase superfamily enzyme that catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA

Released:

Function and Biology Details

Reaction catalysed:
(1a) 3-(methylsulfanyl)acryloyl-CoA + H(2)O = 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-177530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylthioacryloyl-CoA hydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 275 amino acids
Theoretical weight: 29.94 KDa
Source organism: Ruegeria pomeroyi DSS-3
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q5LLW6 (Residues: 1-267; Coverage: 100%)
Gene names: SPO3805, dmdD
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: NSLS BEAMLINE X29A
Spacegroup: P213
Unit cell:
a: 117.66Å b: 117.66Å c: 117.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.135 0.133 0.16
Expression system: Escherichia coli BL21