› 1l6j

X-ray diffraction
2.5Å resolution

Crystal structure of human matrix metalloproteinase MMP9 (gelatinase B).

Released:
DOI: 10.2210/pdb1l6j/pdb
PDB entry 1l6j coloured by chain, front view.
PDB entry 1l6j coloured by chain, side view.
PDB entry 1l6j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase.
Elkins PA, Ho YS, Smith WW, Janson CA, D'Alessio KJ, McQueney MS, Cummings MD, Romanic AM
Acta Crystallogr D Biol Crystallogr 58 1182-92 (2002)
PMID: 12077439

Function and Biology Details

Reaction catalysed: 
Cleavage of gelatin types I and V and collagen types IV and V.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147085 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
67 kDa matrix metalloproteinase-9 Chain: A
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14780 (Residues: 20-444; Coverage: 62%)
Gene names: CLG4B, MMP9
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P65
Unit cell:
a: 123.685Å b: 123.685Å c: 89.937Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 0.23
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Gelatinase-mediated migration and invasion of cancer cells.
Björklund et al. (2005)
13 more

53 mentions without citation

Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities.
Boon et al. (2016)
52 more