› 1t4m

X-ray diffraction
2Å resolution

STRUCTURE OF A THERMOSTABLE DOUBLE MUTANT OF BACILLUS SUBTILIS LIPASE OBTAINED THROUGH DIRECTED EVOLUTION

Released:
DOI: 10.2210/pdb1t4m/pdb
PDB entry 1t4m coloured by chain, front view.
PDB entry 1t4m coloured by chain, side view.
PDB entry 1t4m coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase.
Acharya P, Rajakumara E, Sankaranarayanan R, Rao NM
J Mol Biol 341 1271-81 (2004)
PMID: 15321721

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 Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 19.48 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37957 (Residues: 33-212; Coverage: 99%)
Gene names: BSU02700, estA, lip, lipA
Sequence domains: Lipase (class 2)
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: R3
Unit cell:
a: 76.015Å b: 76.015Å c: 103.093Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.206 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Nature versus nurture: developing enzymes that function under extreme conditions.
Liszka et al. (2012)
9 more

4 mentions without citation

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