4arf

X-ray diffraction
1.77Å resolution

CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM CLOSTRIDIUM HISTOLYTICUM IN COMPLEX WITH THE PEPTIDIC INHIBITOR ISOAMYLPHOSPHONYL-GLY-PRO-ALA AT 1.77 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:
Non-polymer only tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Collagenase ColH Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 45.88 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q46085 (Residues: 331-721; Coverage: 40%)
Gene name: colH
Sequence domains: Collagenase G catalytic helper subdomain
Structure domains:
ISOAMYLPHOSPHONYL-GLY-PRO-ALA Chain: B
Molecule details ›
Chain: B
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: P21212
Unit cell:
a: 79.87Å b: 106.78Å c: 51.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.15 0.2
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided