3eoq

X-ray diffraction
2.29Å resolution

The crystal structure of putative zinc protease beta-subunit from Thermus thermophilus HB8

Released:

Function and Biology Details

Reaction catalysed:
Degradation of insulin, glucagon and other polypeptides. No action on proteins.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177977 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Zinc protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 46.06 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SIV0 (Residues: 1-406; Coverage: 100%)
Gene name: TTHA1264
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 70.34Å b: 94.202Å c: 134.454Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.237
Expression system: Escherichia coli