› 1rtg

X-ray diffraction
2.6Å resolution

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

Released:
DOI: 10.2210/pdb1rtg/pdb
PDB entry 1rtg coloured by chain, front view.
PDB entry 1rtg coloured by chain, side view.
PDB entry 1rtg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
Gohlke U, Gomis-R��th FX, Crabbe T, Murphy G, Docherty AJ, Bode W
FEBS Lett. 378 126-30 (1996)
PMID: 8549817

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140074 (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:
Ligand CL 1 x CL
Ligand CA 2 x CA
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

Quick links

Citations

13 review citations

Matrix metalloproteinases: structures, evolution, and diversification.
Massova et al. (1998)
12 more

8 mentions without citation

Affinity- and specificity-enhancing mutations are frequent in multispecific interactions between TIMP2 and MMPs.
Sharabi et al. (2014)
7 more