PDBe 2ovz

X-ray diffraction
2Å resolution

MMP-9 active site mutant with phosphinate inhibitor

Released:

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:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
67 kDa matrix metalloproteinase-9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14780 (Residues: 110-443; Coverage: 23%)
Gene names: CLG4B, MMP9
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P41212
Unit cell:
a: 55.85Å b: 55.85Å c: 259.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.251
Expression system: Escherichia coli