PDBe 2mzh

Solution NMR

NMR Solution Structure of the PRO Form of Human Matrilysin (proMMP-7) in Complex with Zwitterionic Membrane

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrilysin Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 27.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09237 (Residues: 20-267; Coverage: 99%)
Gene names: MMP7, MPSL1, PUMP1
Sequence domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 44%
Refinement method: molecular dynamics
Chemical shifts: BMR25488  
Expression system: Escherichia coli BL21(DE3)