› 1sio

X-ray diffraction
1.8Å resolution

Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF

Released:
DOI: 10.2210/pdb1sio/pdb
PDB entry 1sio coloured by chain, front view.
PDB entry 1sio coloured by chain, side view.
PDB entry 1sio coloured by chain, top view.
Source organism: Alicyclobacillus sendaiensis
Primary publication:
Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity.
Wlodawer A, Li M, Gustchina A, Tsuruoka N, Ashida M, Minakata H, Oyama H, Oda K, Nishino T, Nakayama T
J Biol Chem 279 21500-10 (2004)
PMID: 15014068

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162444 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S53 domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 364 amino acids
Theoretical weight: 36.72 KDa
Source organism: Alicyclobacillus sendaiensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8GB88 (Residues: 190-553; Coverage: 66%)
Gene name: scpA
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Ace-ILE-PRO-PHL peptide inhibitor Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 4 amino acids
Theoretical weight: 388 Da
Source organism: Alicyclobacillus sendaiensis
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand CA 3 x CA
1 modified residue:
Ligand PHL 3 x PHL

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 49.37Å b: 238.73Å c: 49.25Å
α: 90° β: 113.7° γ: 90°
R-values:
R R work R free
0.173 not available 0.243
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

3 review citations

Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria.
Suzuki et al. (2006)
2 more

4 mentions without citation

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