› 1ck7

X-ray diffraction
2.8Å resolution

GELATINASE A (FULL-LENGTH)

Released:
DOI: 10.2210/pdb1ck7/pdb
PDB entry 1ck7 coloured by chain, front view.
PDB entry 1ck7 coloured by chain, side view.
PDB entry 1ck7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K
Science 284 1667-70 (1999)
PMID: 10356396

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140074 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
72 kDa type IV collagenase Chain: A
Molecule details ›
Chain: A
Length: 631 amino acids
Theoretical weight: 71 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P08253 (Residues: 30-660; Coverage: 100%)
Gene names: CLG4A, MMP2
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 3 x CA
Ligand CL 1 x CL
Ligand NA 1 x NA
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM02
Spacegroup: I4122
Unit cell:
a: 121.32Å b: 121.32Å c: 345.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.286 0.286 0.327
Expression system: Trichoplusia ni

Quick links

Citations

64 review citations

Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
Visse et al. (2003)
63 more

56 mentions without citation

Role of Matrix Metalloproteinases in Angiogenesis and Cancer.
Quintero-Fabián et al. (2019)
55 more