› 6isp

X-ray diffraction
1.88Å resolution

structure of Candida antarctica Lipase B mutant

Released:
DOI: 10.2210/pdb6isp/pdb
PDB entry 6isp coloured by chain, front view.
PDB entry 6isp coloured by chain, side view.
PDB entry 6isp coloured by chain, top view.
Source organism: Moesziomyces antarcticus
Primary publication:
Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution.
Cen Y, Singh W, Arkin M, Moody TS, Huang M, Zhou J, Wu Q, Reetz MT
Nat Commun 10 3198 (2019)
PMID: 31324776

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154386 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 321 amino acids
Theoretical weight: 33.43 KDa
Source organism: Moesziomyces antarcticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41365 (Residues: 26-342; Coverage: 98%)

Ligands and Environments

2 bound ligands:
Ligand CPQ 11 x CPQ
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 46.98Å b: 155.97Å c: 92.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.214 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks.
Godoy et al. (2022)
3 more

3 mentions without citation

Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET.
Magalhães et al. (2021)
2 more