› 3kec

X-ray diffraction
2.05Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagenase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45452 (Residues: 105-267; Coverage: 36%)
Gene name: MMP13
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

5 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 6 x CA
Ligand SO4 2 x SO4
Ligand 3KE 2 x 3KE
Ligand HAE 2 x HAE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21212
Unit cell:
a: 133.209Å b: 72.348Å c: 36.356Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Is there new hope for therapeutic matrix metalloproteinase inhibition?
Vandenbroucke et al. (2014)
8 more

1 mention without citation

Identification of N-Acyl Hydrazones as New Non-Zinc-Binding MMP-13 Inhibitors by Structure-Based Virtual Screening Studies and Chemical Optimization.
Cuffaro et al. (2023)