› 5cri

X-ray diffraction
1.63Å resolution

Wild-type Bacillus subtilis lipase A with 0% [BMIM][Cl]

Released:
DOI: 10.2210/pdb5cri/pdb
PDB entry 5cri coloured by chain, front view.
PDB entry 5cri coloured by chain, side view.
PDB entry 5cri coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.
Nordwald EM, Plaks JG, Snell JR, Sousa MC, Kaar JL
Chembiochem 16 2456-9 (2015)
PMID: 26388426

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 19.38 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
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 SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 39.254Å b: 82.622Å c: 95.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.128 0.164
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Genetic and chemical approaches for surface charge engineering of enzymes and their applicability in biocatalysis: A review.
Pedersen et al. (2019)
2 more

3 mentions without citation

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