› 1thm

X-ray diffraction
1.37Å resolution

CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1thm/pdb
PDB entry 1thm coloured by chain, front view.
PDB entry 1thm coloured by chain, side view.
PDB entry 1thm coloured by chain, top view.
Source organism: Thermoactinomyces vulgaris
Primary publication:
Crystal structure of thermitase at 1.4 A resolution.
Teplyakov AV, Kuranova IP, Harutyunyan EH, Vainshtein BK, Frömmel C, Höhne WE, Wilson KS
J Mol Biol 214 261-79 (1990)
PMID: 2196375

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins, including collagen.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermitase Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 28.37 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Not provided
UniProt:
  • Canonical: P04072 (Residues: 1-279; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand NA 1 x NA
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 72.95Å b: 64.05Å c: 47.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
4 more

31 mentions without citation

Microbial enzymes catalyzing keratin degradation: Classification, structure, function.
Qiu et al. (2020)
30 more