› 1itv

X-ray diffraction
1.95Å resolution

Dimeric form of the haemopexin domain of MMP9

Released:
DOI: 10.2210/pdb1itv/pdb
PDB 1itv coloured by chain and viewed from the front.
PDB 1itv coloured by chain and viewed from the side.
PDB 1itv coloured by chain and viewed from the top.
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)
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

15 review citations

MMP9: A Tough Target for Targeted Therapy for Cancer.
Augoff et al. (2022)
14 more

21 mentions without citation

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