1rtg

X-ray diffraction
2.6Å resolution

C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PEX Chain: A
Molecule details ›
Chain: A
Length: 210 amino acids
Theoretical weight: 23.83 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P08253 (Residues: 451-660; Coverage: 33%)
Gene names: CLG4A, MMP2
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 55.78Å b: 58.85Å c: 93.14Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 not available