› 1sue

X-ray diffraction
1.8Å resolution

SUBTILISIN BPN' FROM BACILLUS AMYLOLIQUEFACIENS, MUTANT

Released:
DOI: 10.2210/pdb1sue/pdb
PDB entry 1sue coloured by chain, front view.
PDB entry 1sue coloured by chain, side view.
PDB entry 1sue coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Mechanism of ionic strength dependence of crystal growth rates in a subtilisin variant.
Gallagher DT, Pan QW, Gilliland GL
J Cryst Growth 193 665-673 (1998)

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin BPN' Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 26.65 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus amyloliquefaciens
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 76%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P212121
Unit cell:
a: 45.59Å b: 58.09Å c: 86.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Bacillus amyloliquefaciens

Quick links

Citations

2 mentions without citation

From the similarity analysis of protein cavities to the functional classification of protein families using cavbase.
Kuhn et al. (2006)
1 more