PDBe 5i12

X-ray diffraction
1.59Å resolution

Crystal structure of the catalytic domain of MMP-9 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).

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 Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14780 (Residues: 113-444; Coverage: 23%)
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: ESRF BEAMLINE ID23-2
Spacegroup: P3221
Unit cell:
a: 39.56Å b: 39.56Å c: 163.55Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.228
Expression system: Escherichia coli