› 1q3a

X-ray diffraction
2.1Å resolution

Crystal structure of the catalytic domain of human matrix metalloproteinase 10

Released:
DOI: 10.2210/pdb1q3a/pdb
PDB entry 1q3a coloured by chain, front view.
PDB entry 1q3a coloured by chain, side view.
PDB entry 1q3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the catalytic domain of human matrix metalloproteinase 10.
Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B
J Mol Biol 336 707-16 (2004)
PMID: 15095982

Function and Biology Details

Reaction catalysed: 
Similar to stromelysin 1, but action on collagen types III, IV and V is weak.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 165 amino acids
Theoretical weight: 18.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09238 (Residues: 99-263; Coverage: 36%)
Gene names: MMP10, STMY2
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 6 x ZN
Ligand CA 9 x CA
Ligand NGH 3 x NGH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 117.152Å b: 61.141Å c: 68.588Å
α: 90° β: 108.68° γ: 90°
R-values:
R R work R free
0.278 0.276 0.298
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

8 mentions without citation

Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities.
Boon et al. (2016)
7 more