› 1zvj

X-ray diffraction
2.03Å resolution

Structure of Kumamolisin-AS mutant, D164N

Released:
DOI: 10.2210/pdb1zvj/pdb
PDB entry 1zvj coloured by chain, front view.
PDB entry 1zvj coloured by chain, side view.
PDB entry 1zvj coloured by chain, top view.
Source organism: Alicyclobacillus sendaiensis
Primary publication:
Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active site.
Okubo A, Li M, Ashida M, Oyama H, Gustchina A, Oda K, Dunn BM, Wlodawer A, Nakayama T
FEBS J 273 2563-76 (2006)
PMID: 16704427

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kumamolisin-As Chain: A
Molecule details ›
Chain: A
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

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 41.85Å b: 44.66Å c: 49.07Å
α: 114.9° β: 105.9° γ: 102.1°
R-values:
R R work R free
0.188 0.184 0.263
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.
Zhang et al. (2015)
6 other articles