› 5ue4

X-ray diffraction
1.8Å resolution

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:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-147085 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
67 kDa matrix metalloproteinase-9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 26.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14780 (Residues: 35-445; Coverage: 34%)
Gene names: CLG4B, MMP9
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

4 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 5 x CA
Ligand SO4 3 x SO4
Ligand 5XQ 1 x 5XQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 89.82Å b: 72.945Å c: 77.537Å
α: 90° β: 106.91° γ: 90°
R-values:
R R work R free
0.2 0.199 0.224
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Targeting Tumor Microenvironment for Cancer Therapy.
Roma-Rodrigues et al. (2019)
25 more

10 mentions without citation

Harnessing protein folding neural networks for peptide-protein docking.
Tsaban et al. (2022)
9 more