› 4gxn

X-ray diffraction
2.2Å resolution

Diethylphosphonate Inhibited Structure of the Proteus mirabilis Lipase

Released:
DOI: 10.2210/pdb4gxn/pdb
PDB entry 4gxn coloured by chain, front view.
PDB entry 4gxn coloured by chain, side view.
PDB entry 4gxn coloured by chain, top view.
Source organism: Proteus mirabilis
Primary publication:
Crystal structure of Proteus mirabilis lipase, a novel lipase from the Proteus/psychrophilic subfamily of lipase family I.1.
Korman TP, Bowie JU
PLoS One 7 e52890 (2012)
PMID: 23300806

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 33.85 KDa
Source organism: Proteus mirabilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: B4EVM3 (Residues: 1-287; Coverage: 100%)
Gene name: PMI0999
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand DEP 1 x DEP
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P32
Unit cell:
a: 65.574Å b: 65.574Å c: 63.465Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.195 0.249
Expression system: Escherichia coli BL21

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Citations

1 review citation

An Appraisal on Prominent Industrial and Biotechnological Applications of Bacterial Lipases.
Akram et al. (2023)
5 other articles

4 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
3 more