PDBe 4hma

X-ray diffraction
1.94Å resolution

Crystal structure of an MMP twin carboxylate based inhibitor LC20 in complex with the MMP-9 catalytic domain

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
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14780 (Residues: 110-444; Coverage: 23%)
Gene names: CLG4B, MMP9

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 73.87Å b: 98.24Å c: 47.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.283
Expression system: Escherichia coli