› 1gt9

X-ray diffraction
1.38Å resolution

High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)

Released:
DOI: 10.2210/pdb1gt9/pdb
PDB entry 1gt9 coloured by chain, front view.
PDB entry 1gt9 coloured by chain, side view.
PDB entry 1gt9 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase.
Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W
Structure 10 865-76 (2002)
PMID: 12057200

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S53 domain-containing protein Chains: 1, 2
Molecule details ›
Chains: 1, 2
Length: 357 amino acids
Theoretical weight: 36.32 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RR56 (Residues: 189-545; Coverage: 65%)
Gene name: kscp
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 54.86Å b: 78.25Å c: 73.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.208
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
Ekici et al. (2008)
2 more

5 mentions without citation

A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases.
Wlodawer et al. (2003)
4 more