› 5ct9

X-ray diffraction
1.4Å resolution

G158E/K44E/R57E/Y49E Bacillus subtilis lipase A with 5% [BMIM][Cl]

Released:
DOI: 10.2210/pdb5ct9/pdb
PDB entry 5ct9 coloured by chain, front view.
PDB entry 5ct9 coloured by chain, side view.
PDB entry 5ct9 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 Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 19.32 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

2 bound ligands:
Ligand CL 1 x CL
Ligand BM0 1 x BM0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 48.14Å b: 55.9Å c: 64.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.126 0.124 0.154
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

2 mentions without citation

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