› 1au9

X-ray diffraction
1.8Å resolution

SUBTILISIN BPN' MUTANT 8324 IN CITRATE

Released:
DOI: 10.2210/pdb1au9/pdb
PDB entry 1au9 coloured by chain, front view.
PDB entry 1au9 coloured by chain, side view.
PDB entry 1au9 coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.
Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN
Biochemistry 28 7205-13 (1989)
PMID: 2684274

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: 275 amino acids
Theoretical weight: 27.51 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand UNX 2 x UNX
Ligand IPA 2 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P21
Unit cell:
a: 41.64Å b: 79.45Å c: 37.26Å
α: 90° β: 114.53° γ: 90°
R-values:
R R work R free
0.151 0.151 not available
Expression system: Bacillus subtilis

Quick links

Citations

14 review citations

Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution.
Lehmann et al. (2001)
13 more

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