› 6kjd

X-ray diffraction
2.3Å resolution

lovastatin esterase PcEST inactive mutant S57A in complex with lovastatin

Released:
DOI: 10.2210/pdb6kjd/pdb
PDB 6kjd coloured by chain and viewed from the front.
PDB 6kjd coloured by chain and viewed from the side.
PDB 6kjd coloured by chain and viewed from the top.
Source organism: Penicillium rubens Wisconsin 54-1255
Primary publication:
Structural insights into the catalytic mechanism of lovastatin hydrolase
Liang YJ, Lu XF
J. Biol. Chem. (2019)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lovastatin esterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 400 amino acids
Theoretical weight: 43.46 KDa
Source organism: Penicillium rubens Wisconsin 54-1255
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B6H6L7 (Residues: 1-399; Coverage: 100%)
Gene names: PCH_Pc15g00720, Pc15g00720, PcEST
Sequence domains: Beta-lactamase

Ligands and Environments

2 bound ligands:
Ligand LVA 2 x LVA
Ligand 144 5 x 144
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P212121
Unit cell:
a: 87.909Å b: 91.016Å c: 139.849Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.21
Expression system: Escherichia coli BL21(DE3)

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