1ndu

X-ray diffraction
1.6Å resolution

Bacillus lentus subtilisin variant S101G/V104N

Released:
Source organism: Lederbergia lenta
Primary publication:
Subtilisin surface properties and crystal growth kinetics
J Cryst Growth 254 492-502 (2003)

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:
Cellular component:

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: 26.73 KDa
Source organism: Lederbergia lenta
Expression system: Not provided
UniProt:
  • Canonical: P29600 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 47.75Å b: 62.5Å c: 75.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.222
Expression system: Not provided