› 1gtg

X-ray diffraction
2.3Å resolution

Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)

Released:
DOI: 10.2210/pdb1gtg/pdb
PDB entry 1gtg coloured by chain, front view.
PDB entry 1gtg coloured by chain, side view.
PDB entry 1gtg coloured by chain, top view.
Source organism: Bacillus sp. MN-32
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S53 domain-containing protein Chain: 1
Molecule details ›
Chain: 1
Length: 357 amino acids
Theoretical weight: 36.32 KDa
Source organism: Bacillus sp. MN-32
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 42.63Å b: 78.32Å c: 49Å
α: 90° β: 106.33° γ: 90°
R-values:
R R work R free
0.206 0.206 0.259
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

1 mention without citation

Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Guhaniyogi et al. (2009)