› 1mmq

X-ray diffraction
1.9Å resolution

MATRILYSIN COMPLEXED WITH HYDROXAMATE INHIBITOR

Released:
DOI: 10.2210/pdb1mmq/pdb
PDB entry 1mmq coloured by chain, front view.
PDB entry 1mmq coloured by chain, side view.
PDB entry 1mmq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Matrilysin-inhibitor complexes: common themes among metalloproteases.
Browner MF, Smith WW, Castelhano AL
Biochemistry 34 6602-10 (1995)
PMID: 7756291

Function and Biology Details

Reaction catalysed: 
Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrilysin Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 18.74 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P09237 (Residues: 95-264; Coverage: 68%)
Gene names: MMP7, MPSL1, PUMP1
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 RRS 1 x RRS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 61.9Å b: 61.9Å c: 88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Cricetulus griseus

Quick links

Citations

22 review citations

Matrix metalloproteinases: structures, evolution, and diversification.
Massova et al. (1998)
21 more

13 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
12 more