4are

X-ray diffraction
2.19Å resolution

Crystal structure of the collagenase Unit of collagenase G from Clostridium histolyticum at 2.19 angstrom resolution.

Released:

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-194955 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagenase ColG Chain: A
Molecule details ›
Chain: A
Length: 695 amino acids
Theoretical weight: 79.48 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X721 (Residues: 119-789; Coverage: 63%)
Gene name: colG
Sequence domains:
Structure domains: Threonyl-tRNA Synthetase; Chain A, domain 2

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 55.29Å b: 108.66Å c: 181Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.243
Expression system: Escherichia coli BL21(DE3)