PDBe 1qib

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF GELATINASE A CATALYTIC DOMAIN

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
72 kDa type IV collagenase Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 17.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08253 (Residues: 115-213, 394-449; Coverage: 25%)
Gene names: CLG4A, MMP2
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS
Spacegroup: P4122
Unit cell:
a: 84.83Å b: 84.83Å c: 57.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.244
Expression system: Escherichia coli