PDBe 4auo

X-ray diffraction
3Å resolution

Crystal structure of MMP-1(E200A) in complex with a triple-helical collagen peptide

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Interstitial collagenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 42.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03956 (Residues: 100-466; Coverage: 82%)
Gene names: CLG, MMP1
Sequence domains:
Structure domains:
TRIPLE-HELICAL COLLAGEN PEPTIDE Chains: C, D, E, F, G, H
Molecule details ›
Chains: C, D, E, F, G, H
Length: 40 amino acids
Theoretical weight: 3.78 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
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P2
Unit cell:
a: 76.671Å b: 102.241Å c: 80.734Å
α: 90° β: 103.75° γ: 90°
R-values:
R R work R free
0.211 0.211 0.273
Expression systems:
  • Escherichia coli
  • Not provided