1Q3A

Crystal structure of the catalytic domain of human matrix metalloproteinase 10

Summary for 1Q3A

• Entry DOI: 10.2210/pdb1q3a/pdb
• Related: 1BQO 1D5J 1D8F 1G49 1UEA
• Descriptor: Stromelysin-2, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: mmp-10, metalloproteinase, inhibitors, nngh, stromelysin-2, hydroxamic acid, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 57314.74

Authors

Calderone, V.,Bertini, I.,Fragai, M.,Luchinat, C.,Mangani, S.,Terni, B. (deposition date: 2003-07-29, release date: 2004-04-06, Last modification date: 2023-08-16)

Primary citation

Bertini, I.,Calderone, V.,Fragai, M.,Luchinat, C.,Mangani, S.,Terni, B.
Crystal structure of the catalytic domain of human matrix metalloproteinase 10.
J.Mol.Biol., 336:707-716, 2004

PubMed Abstract: The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 A resolution. The availability of this structure allowed us to critically examine the small differences existing between the catalytic domains of MMP-3 and MMP-10, which show the highest sequence identity among all MMPs. Furthermore, the binding mode of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time.

PubMed: 15095982
DOI: 10.1016/j.jmb.2003.12.033

Experimental method

X-RAY DIFFRACTION (2.1 Å)