X-ray diffraction
2.05Å resolution

Crystal structure of the peptidase domain of collagenase T from Clostridium tetani complexed with the peptidic inhibitor isoamyl- phosphonyl-Gly-Pro-Ala at 2.05 angstrom resolution.


Function and Biology Details

Reaction catalysed:
Digestion of native collagen in the triple helical region at -|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Collagenase ColT Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 45.75 KDa
Source organism: Clostridium tetani
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q899Y1 (Residues: 340-730; Coverage: 41%)
Gene names: CTC_p33, colT
Structure domains:
Molecule details ›
Chains: C, D
Length: 4 amino acids
Theoretical weight: 391 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 74.42Å b: 102.08Å c: 102.48Å
α: 90° β: 90° γ: 90°
R R work R free
0.22 0.218 0.268
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided