› 1rm8

X-ray diffraction
1.8Å resolution

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features

Released:
DOI: 10.2210/pdb1rm8/pdb
PDB entry 1rm8 coloured by chain, front view.
PDB entry 1rm8 coloured by chain, side view.
PDB entry 1rm8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features.
Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K
J Mol Biol 336 213-25 (2004)
PMID: 14741217

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-156344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrix metalloproteinase-16 Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 18.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P51512 (Residues: 124-292; Coverage: 29%)
Gene names: C8orf57, MMP16, MMPX2
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P4322
Unit cell:
a: 51.21Å b: 51.21Å c: 149.368Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.236
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Physiology and pathophysiology of matrix metalloproteases.
Klein et al. (2011)
6 more

8 mentions without citation

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