PDBe 4h1q

X-ray diffraction
1.59Å 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:
monomeric (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 BL21(DE3)
UniProt:
  • Canonical: P14780 (Residues: 110-444; Coverage: 23%)
Gene names: CLG4B, MMP9

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 44.14Å b: 48.66Å c: 67.92Å
α: 90° β: 102.55° γ: 90°
R-values:
R R work R free
0.172 0.17 0.211
Expression system: Escherichia coli BL21(DE3)