› 2qxu

X-ray diffraction
1.9Å resolution

Crystal Structure Analysis of the Bacillus subtilis lipase crystallized at pH 5.0

Released:
DOI: 10.2210/pdb2qxu/pdb
PDB entry 2qxu coloured by chain, front view.
PDB entry 2qxu coloured by chain, side view.
PDB entry 2qxu coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH.
Rajakumara E, Acharya P, Ahmad S, Sankaranaryanan R, Rao NM
Biochim Biophys Acta 1784 302-11 (2008)
PMID: 18053819

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-153519 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase EstA Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 179 amino acids
Theoretical weight: 19.18 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37957 (Residues: 34-212; Coverage: 99%)
Gene names: BSU02700, estA, lip, lipA
Sequence domains: Lipase (class 2)
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 218.608Å b: 110.934Å c: 51.988Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.211 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Thermally denatured state determines refolding in lipase: mutational analysis.
Ahmad et al. (2009)
5 more

3 mentions without citation

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