› 1itv

X-ray diffraction
1.95Å resolution

Dimeric form of the haemopexin domain of MMP9

Released:
DOI: 10.2210/pdb1itv/pdb
PDB entry 1itv coloured by chain, front view.
PDB entry 1itv coloured by chain, side view.
PDB entry 1itv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of the adaptive molecular recognition by MMP9.
Cha H, Kopetzki E, Huber R, Lanzendörfer M, Brandstetter H
J Mol Biol 320 1065-79 (2002)
PMID: 12126625

Function and Biology Details

Reaction catalysed: 
Cleavage of gelatin types I and V and collagen types IV and V.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
82 kDa matrix metalloproteinase-9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 195 amino acids
Theoretical weight: 22.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14780 (Residues: 513-707; Coverage: 28%)
Gene names: CLG4B, MMP9
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43
Unit cell:
a: 127.72Å b: 127.72Å c: 31.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.229 0.275
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

22 mentions without citation

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