PDBe 4h82

X-ray diffraction
1.9Å resolution

Crystal structure of mutant MMP-9 catalytic domain in complex with a twin 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

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
67 kDa matrix metalloproteinase-9 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 160 amino acids
Theoretical weight: 17.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14780 (Residues: 110-444; 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: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P1
Unit cell:
a: 39.9Å b: 98.86Å c: 47.13Å
α: 90.03° β: 111.95° γ: 89.98°
R-values:
R R work R free
0.209 0.207 0.241
Expression system: Escherichia coli BL21(DE3)