› 1isp

X-ray diffraction
1.3Å resolution

Crystal structure of Bacillus subtilis lipase at 1.3A resolution

Released:
DOI: 10.2210/pdb1isp/pdb
PDB entry 1isp coloured by chain, front view.
PDB entry 1isp coloured by chain, side view.
PDB entry 1isp coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.
Kawasaki K, Kondo H, Suzuki M, Ohgiya S, Tsuda S
Acta Crystallogr D Biol Crystallogr 58 1168-74 (2002)
PMID: 12077437

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: 19.38 KDa
Source organism: Bacillus subtilis
Expression system: Priestia megaterium
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 GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 38.2Å b: 58.45Å c: 82.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.232
Expression system: Priestia megaterium

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Citations

1 review citation

Stabilizing biocatalysts.
Bommarius et al. (2013)
21 other articles

13 mentions without citation

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