PDBe 4h2e

X-ray diffraction
2.9Å resolution

Crystal structure of an MMP twin inhibitor complexing two MMP-9 catalytic domains

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
67 kDa matrix metalloproteinase-9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14780 (Residues: 107-444; Coverage: 24%)
Gene names: CLG4B, MMP9
Sequence domains: Matrixin
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: P21
Unit cell:
a: 40.18Å b: 97.4Å c: 45.69Å
α: 90° β: 111.99° γ: 90°
R-values:
R R work R free
0.279 0.277 0.311
Expression system: Escherichia coli BL21(DE3)