1sv6

X-ray diffraction
2.9Å resolution

Crystal structure of 2-hydroxypentadienoic acid hydratase from Escherichia Coli

Released:
Source organism: Escherichia coli
Entry authors: Fedorov AA, Fedorov EV, Sharp A, Almo SC, Burley SK, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
(S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-dienoate + H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-160184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-keto-4-pentenoate hydratase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 269 amino acids
Theoretical weight: 28.92 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77608 (Residues: 1-269; Coverage: 100%)
Gene names: JW0341, b0350, mhpD
Sequence domains: Fumarylacetoacetate (FAA) hydrolase family
Structure domains: Fumarylacetoacetase-like, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P21
Unit cell:
a: 55.222Å b: 121.507Å c: 111.796Å
α: 90° β: 94.1° γ: 90°
R-values:
R R work R free
0.243 0.239 0.267
Expression system: Escherichia coli