› 1ggv

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE PROTEASE INHIBITOR, PHENYLMETHYLSULFONYL FLUORIDE (PMSF)

Released:
DOI: 10.2210/pdb1ggv/pdb
PDB entry 1ggv coloured by chain, front view.
PDB entry 1ggv coloured by chain, side view.
PDB entry 1ggv coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF).
Robinson A, Edwards KJ, Carr PD, Barton JD, Ewart GD, Ollis DL
Acta Crystallogr D Biol Crystallogr 56 1376-84 (2000)
PMID: 11053834

Function and Biology Details

Reaction catalysed: 
4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxymethylenebutenolidase Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 25.12 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A114 (Residues: 1-232; Coverage: 98%)
Gene name: clcD
Sequence domains: Dienelactone hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SEB 1 x SEB

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 51.08Å b: 51.86Å c: 82.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.151 not available
Expression system: Escherichia coli

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Citations

4 citation in other articles

The thioesterase domain of the fengycin biosynthesis cluster: a structural base for the macrocyclization of a non-ribosomal lipopeptide.
Samel et al. (2006)
3 more

1 mention without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)