1gen

X-ray diffraction
2.15Å resolution

C-TERMINAL DOMAIN OF GELATINASE A

Released:
Source organism: Homo sapiens

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PEX Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 24.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08253 (Residues: 443-660; Coverage: 35%)
Gene names: CLG4A, MMP2
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 57.9Å b: 77.4Å c: 53.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.26
Expression system: Escherichia coli