› 1uka

X-ray diffraction
1.7Å resolution

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

Released:
DOI: 10.2210/pdb1uka/pdb
PDB 1uka coloured by chain and viewed from the front.
PDB 1uka coloured by chain and viewed from the side.
PDB 1uka coloured by chain and viewed from the top.
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:
  • not assigned
Sequence domains:
Structure domain:

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:
Ligand SMB 1 x SMB
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

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Citations

1 review citation

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