› 1gnv

X-ray diffraction
1.9Å resolution

CALCIUM INDEPENDENT SUBTILISIN BPN' MUTANT

Released:
DOI: 10.2210/pdb1gnv/pdb
PDB entry 1gnv coloured by chain, front view.
PDB entry 1gnv coloured by chain, side view.
PDB entry 1gnv coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.
Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL
J Biol Chem 277 27553-8 (2002)
PMID: 12011071

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: 26.77 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 76%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MIS 1 x MIS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 54.2Å b: 60.4Å c: 82.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Directed evolution of enzyme stability.
Eijsink et al. (2005)
19 other articles

2 mentions without citation

From thiol-subtilisin to omniligase: Design and structure of a broadly applicable peptide ligase.
Toplak et al. (2021)
1 more