PDBe 2n8r

Solution NMR

Productive complex between MMP-12 and synthetic triple-helical collagen, revealed through paramagnetic NMR

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Macrophage metalloelastase Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39900 (Residues: 100-263; Coverage: 36%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Collagen triple helix repeat family protein Chains: B, C, D
Molecule details ›
Chains: B, C, D
Length: 36 amino acids
Theoretical weight: 3.29 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 59%
Refinement method: Rigid-body docking, Conformer selection
Chemical shifts: BMR25859  
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided