› 1zvk

X-ray diffraction
2.04Å resolution

Structure of Double mutant, D164N, E78H of Kumamolisin-As

Released:
DOI: 10.2210/pdb1zvk/pdb
PDB entry 1zvk coloured by chain, front view.
PDB entry 1zvk coloured by chain, side view.
PDB entry 1zvk 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:
Peptidase S53 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 36.12 KDa
Source organism: Alicyclobacillus sendaiensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8GB88 (Residues: 190-547; Coverage: 65%)
Gene name: scpA
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 58.05Å b: 74.81Å c: 78.38Å
α: 90° β: 103.08° γ: 90°
R-values:
R R work R free
0.188 0.188 0.292
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