› 1t1e

X-ray diffraction
1.18Å resolution

High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)

Released:
DOI: 10.2210/pdb1t1e/pdb
PDB entry 1t1e coloured by chain, front view.
PDB entry 1t1e coloured by chain, side view.
PDB entry 1t1e coloured by chain, top view.
Source organism: Bacillus sp. MN-32
Primary publication:
1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase.
Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W
Structure 12 1313-23 (2004)
PMID: 15242607

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S53 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 552 amino acids
Theoretical weight: 57.75 KDa
Source organism: Bacillus sp. MN-32
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RR56 (Residues: 1-552; Coverage: 100%)
Gene name: kscp
Sequence domains:
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: R32
Unit cell:
a: 158.64Å b: 158.64Å c: 106.72Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.244
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin.
Shinde et al. (2011)
2 more

8 mentions without citation

Computational design of an α-gliadin peptidase.
Gordon et al. (2012)
7 more