3whi

X-ray diffraction
2.4Å resolution

Crystal structure of unautoprocessed form of IS1-inserted Pro-subtilisin E

Released:

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-137496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin E Chains: A, B
Molecule details ›
Chains: A, B
Length: 365 amino acids
Theoretical weight: 37.47 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P04189 (Residues: 30-106, 107-381; Coverage: 100%)
Gene names: BSU10300, apr, aprA, aprE, sprE
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P6522
Unit cell:
a: 135.202Å b: 135.202Å c: 151.606Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.198 0.27
Expression system: Escherichia coli