X-ray diffraction
2.55Å resolution

Crystal structure of apo collagenase G from Clostridium histolyticum at 2.55 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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Collagenase ColG Chain: A
Molecule details ›
Chain: A
Length: 785 amino acids
Theoretical weight: 89.59 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli
  • Canonical: Q9X721 (Residues: 119-880; Coverage: 71%)
Gene name: colG
Sequence domains:
Structure domains: Threonyl-tRNA Synthetase; Chain A, domain 2

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 56.96Å b: 109.05Å c: 182.46Å
α: 90° β: 90° γ: 90°
R R work R free
0.21 0.208 0.256
Expression system: Escherichia coli