› 4c3u

X-ray diffraction
2.29Å resolution

Extensive counter-ion interactions with subtilisin in aqueous medium, Cs derivative

Released:
DOI: 10.2210/pdb4c3u/pdb
Model geometry
Fit model/data
PDB entry 4c3u coloured by chain, front view.
PDB entry 4c3u coloured by chain, side view.
PDB entry 4c3u coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Extensive Counter-Ion Interactions Seen at the Surface of Subtilisin in an Aqueous Medium
Cianci M, Negroni J, Helliwell JR, Halling PJ
RSC Adv (2014)

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

4 bound ligands:
Ligand CL 6 x CL
Ligand CS 10 x CS
Ligand CA 1 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 52.167Å b: 55.226Å c: 75.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.156 0.234

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