6cm1

Solution NMR

MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs

Released:
Source organism: Homo sapiens
Entry authors: Marcink TC, Van Doren SR

Function and Biology Details

Reaction catalysed:
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Matrix metalloproteinase-14 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50281 (Residues: 316-511; Coverage: 35%)
Gene name: MMP14
Structure domains: Hemopexin-like domain
Truncated apolipoprotein A-I Chains: B, C
Molecule details ›
Chains: B, C
Length: 211 amino acids
Theoretical weight: 24.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02647 (Residues: 79-122, 123-267; Coverage: 76%)
Gene name: APOA1
Sequence domains: Apolipoprotein A1/A4/E domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 3%
Refinement method: molecular dynamics
Expression system: Escherichia coli