› 1r4z

X-ray diffraction
1.8Å resolution

Bacillus subtilis lipase A with covalently bound Rc-IPG-phosphonate-inhibitor

Released:
DOI: 10.2210/pdb1r4z/pdb
PDB entry 1r4z coloured by chain, front view.
PDB entry 1r4z coloured by chain, side view.
PDB entry 1r4z coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection.
Dröge MJ, Boersma YL, van Pouderoyen G, Vrenken TE, Rüggeberg CJ, Reetz MT, Dijkstra BW, Quax WJ
Chembiochem 7 149-57 (2006)
PMID: 16342303

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153519 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase EstA Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 19.38 KDa
Source organism: Bacillus subtilis
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P37957 (Residues: 32-212; Coverage: 100%)
Gene names: BSU02700, estA, lip, lipA
Sequence domains: Lipase (class 2)
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand RIL 2 x RIL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 39.489Å b: 83.318Å c: 94.638Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.21
Expression system: Bacillus subtilis

Quick links

Citations

5 review citations

Protein engineering of α/β-hydrolase fold enzymes.
Jochens et al. (2011)
4 more

5 mentions without citation

The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.
Khan et al. (2017)
4 more