› 1uk8

X-ray diffraction
1.6Å resolution

Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-valerate

Released:
DOI: 10.2210/pdb1uk8/pdb
PDB entry 1uk8 coloured by chain, front view.
PDB entry 1uk8 coloured by chain, side view.
PDB entry 1uk8 coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products.
Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T
Biosci Biotechnol Biochem 69 491-8 (2005)
PMID: 15784976

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-551675 (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:
Ligand LEA 2 x LEA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2221
Unit cell:
a: 77.101Å b: 116.001Å c: 78.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.19
Expression system: Escherichia coli

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Citations

1 review citation

Biodegradation of aromatic compounds: an overview of meta-fission product hydrolases.
Khajamohiddin et al. (2008)
6 other articles