› 3d2a

X-ray diffraction
1.73Å resolution

Structure of 1-17A4, a thermostable mutant of Bacillus subtilis lipase obtained through directed evolution

Released:
DOI: 10.2210/pdb3d2a/pdb
PDB entry 3d2a coloured by chain, front view.
PDB entry 3d2a coloured by chain, side view.
PDB entry 3d2a coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight.
Ahmad S, Kamal MZ, Sankaranarayanan R, Rao NM
J Mol Biol 381 324-40 (2008)
PMID: 18599073

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 19.48 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 38.014Å b: 57.958Å c: 82.849Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.221
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Thermophilic proteins: insight and perspective from in silico experiments.
Sterpone et al. (2012)
7 more

5 mentions without citation

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