› 2wuv

X-ray diffraction
2.24Å resolution

Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile

Released:
DOI: 10.2210/pdb2wuv/pdb
PDB entry 2wuv coloured by chain, front view.
PDB entry 2wuv coloured by chain, side view.
PDB entry 2wuv coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Crystallographic analysis of counterion effects on subtilisin enzymatic action in acetonitrile.
Cianci M, Tomaszewski B, Helliwell JR, Halling PJ
J Am Chem Soc 132 2293-300 (2010)
PMID: 20099851

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Carlsberg Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus licheniformis
UniProt:
  • Canonical: P00780 (Residues: 106-379; Coverage: 78%)
Gene names: apr, subC
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

5 bound ligands:
Ligand CL 8 x CL
Ligand CS 11 x CS
Ligand CA 1 x CA
Ligand NA 1 x NA
Ligand CCN 5 x CCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 52.177Å b: 55.311Å c: 75.778Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.231

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Citations

3 citation in other articles

A molecular perspective on nonaqueous biocatalysis: contributions from simulation studies.
Lousa et al. (2013)
2 more

1 mention without citation

Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site.
Arai et al. (2015)