1uka

X-ray diffraction
1.7Å resolution

Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with (S)-2-methylbutyrate

Released:

Function and Biology Details

Reaction catalysed:
2-hydroxymuconate-6-semialdehyde + H(2)O = formate + 2-oxopent-4-enoate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 31.51 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P96965 (Residues: 1-282; Coverage: 100%)
Gene name: cumD
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2221
Unit cell:
a: 77.019Å b: 116.444Å c: 78.562Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.196
Expression system: Escherichia coli