› 2jsd

Solution NMR

Solution structure of MMP20 complexed with NNGH

Released:
DOI: 10.2210/pdb2jsd/pdb
PDB entry 2jsd coloured by chain, ensemble of 20 models, front view.
PDB entry 2jsd coloured by chain, ensemble of 20 models, side view.
PDB entry 2jsd coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
Arendt Y, Banci L, Bertini I, Cantini F, Cozzi R, Del Conte R, Gonnelli L
FEBS Lett 581 4723-6 (2007)
PMID: 17869250

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-130110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrix metalloproteinase-20 Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O60882 (Residues: 113-272; Coverage: 35%)
Gene name: MMP20
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand ZN 2 x ZN
Ligand NGH 1 x NGH
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Arylsulfonamides and selectivity of matrix metalloproteinase-2: An overview.
Adhikari et al. (2017)
1 more