› 4cg0

X-ray diffraction
1.36Å resolution

Savinase crystal structures for combined single crystal diffraction and powder diffraction analysis

Released:
DOI: 10.2210/pdb4cg0/pdb
PDB entry 4cg0 coloured by chain, front view.
PDB entry 4cg0 coloured by chain, side view.
PDB entry 4cg0 coloured by chain, top view.
Source organism: Lederbergia lenta
Primary publication:
Analysis of an industrial production suspension of Bacillus lentus subtilisin crystals by powder diffraction: a powerful quality-control tool.
Frankaer CG, Moroz OV, Turkenburg JP, Aspmo SI, Thymark M, Friis EP, Stahl K, Nielsen JE, Wilson KS, Harris P
Acta Crystallogr D Biol Crystallogr 70 1115-23 (2014)
PMID: 24699655

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151551 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Savinase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 26.72 KDa
Source organism: Lederbergia lenta
Expression system: Bacillus licheniformis
UniProt:
  • Canonical: P29600 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 53.04Å b: 57.55Å c: 71.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.111 0.109 0.154
Expression system: Bacillus licheniformis

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Citations

1 citations in other articles

Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis.
Wu et al. (2020)