1RTG: C-terminal Domain (haemopexin-like Domain) Of Human Matrix Metalloproteinase-2

Citation:
Abstract
In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
PDB ID: 1RTGDownload
MMDB ID: 57319
PDB Deposition Date: 1995/12/21
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 1RTG: monomeric; determined by author
Molecular Components in 1RTG
Label Count Molecule
Protein (1 molecule)
1
Human Gelatinase a(Gene symbol: MMP2)
Molecule annotation
Chemicals (3 molecules)
1
1
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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