2K2G
Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor
Summary for 2K2G
Entry DOI | 10.2210/pdb2k2g/pdb |
Descriptor | Macrophage metalloelastase, ZINC ION, N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine (3 entities in total) |
Functional Keywords | macrophage elastase, matrix metalloproteinase, protein-ligand structure, catalytic domain, human gene, calcium, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen |
Biological source | Homo sapiens (Human) |
Cellular location | Secreted, extracellular space, extracellular matrix (Probable): P39900 |
Total number of polymer chains | 1 |
Total formula weight | 18860.87 |
Authors | Markus, M.A.,Dwyer, B.,Wolfrom, S.,Li, J.,Li, W.,Malakian, K.,Wilhelm, J.,Tsao, D.H.H. (deposition date: 2008-04-01, release date: 2008-05-20, Last modification date: 2024-05-29) |
Primary citation | Markus, M.A.,Dwyer, B.,Wolfrom, S.,Li, J.,Li, W.,Malakian, K.,Wilhelm, J.,Tsao, D.H. Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor. J.Biomol.Nmr, 41:55-60, 2008 Cited by PubMed: 18425585DOI: 10.1007/s10858-008-9236-4 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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