PDBe 3ayu

X-ray diffraction
2Å resolution

Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Soluble APP-beta Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.08 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 586-595; Coverage: 1%)
Gene names: A4, AD1, APP
72 kDa type IV collagenase Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 18.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08253 (Residues: 110-450; Coverage: 27%)
Gene names: CLG4A, MMP2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: Cu FINE FOCUS
Spacegroup: P212121
Unit cell:
a: 61.881Å b: 76.06Å c: 37.082Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.205
Expression systems:
  • Not provided
  • Escherichia coli