X-ray diffraction
2.18Å resolution

Structure of 4D3, a thermostable mutant of Bacillus subtilis lipase obtained through directed evolution


Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo 24-mer
Entry contents:
1 distinct polypeptide molecule
Lipase EstA Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 181 amino acids
Theoretical weight: 19.6 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P37957 (Residues: 32-212; Coverage: 100%)
Gene names: BSU02700, estA, lip, lipA
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: C2221
Unit cell:
a: 132.285Å b: 198.042Å c: 197.902Å
α: 90° β: 90° γ: 90°
R R work R free
0.202 0.202 0.245
Expression system: Escherichia coli