› 1cxv

X-ray diffraction
2Å resolution

STRUCTURE OF RECOMBINANT MOUSE COLLAGENASE-3 (MMP-13)

Released:
DOI: 10.2210/pdb1cxv/pdb
PDB entry 1cxv coloured by chain, front view.
PDB entry 1cxv coloured by chain, side view.
PDB entry 1cxv coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure of recombinant mouse collagenase-3 (MMP-13).
Botos I, Meyer E, Swanson SM, Lemaître V, Eeckhout Y, Meyer EF
J Mol Biol 292 837-44 (1999)
PMID: 10525409

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152615 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagenase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.52 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P33435 (Residues: 105-268; Coverage: 36%)
Gene name: Mmp13
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 4 x CA
Ligand CBP 2 x CBP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 56.36Å b: 48.46Å c: 74.94Å
α: 90° β: 108.15° γ: 90°
R-values:
R R work R free
0.196 0.196 0.234

Quick links

Citations

3 review citations

Geometry of nonbonded interactions involving planar groups in proteins.
Chakrabarti et al. (2007)
2 more

5 mentions without citation

Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.
Sinha et al. (2008)
4 more