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1G4K

X-ray Structure of a Novel Matrix Metalloproteinase Inhibitor Complexed to Stromelysin

Summary for 1G4K
Entry DOI10.2210/pdb1g4k/pdb
DescriptorSTROMELYSIN-1, ZINC ION, CALCIUM ION, ... (6 entities in total)
Functional Keywordsstomelysin, mmp, zinc ligand, hydrolase
Biological sourceHomo sapiens (human)
Total number of polymer chains3
Total formula weight58437.25
Authors
Dunten, P.,Kammlott, U.,Crowther, R.,Levin, W.,Foley, L.H.,Wang, P.,Palermo, R. (deposition date: 2000-10-27, release date: 2001-04-25, Last modification date: 2024-02-07)
Primary citationDunten, P.,Kammlott, U.,Crowther, R.,Levin, W.,Foley, L.H.,Wang, P.,Palermo, R.
X-ray structure of a novel matrix metalloproteinase inhibitor complexed to stromelysin.
Protein Sci., 10:923-926, 2001
Cited by
PubMed Abstract: A new class of matrix metalloproteinase (MMP) inhibitors has been identified by screening a collection of compounds against stromelysin. The inhibitors, 2,4,6-pyrimidine triones, have proven to be potent inhibitors of gelatinases A and B. An X-ray crystal structure of one representative compound bound to the catalytic domain of stromelysin shows that the compounds bind at the active site and ligand the active-site zinc. The pyrimidine triones mimic substrates in forming hydrogen bonds to key residues in the active site, and provide opportunities for placing appropriately chosen groups into the S1' specificity pocket of MMPS: A number of compounds have been synthesized and assayed against stromelysin, and the variations in potency are explained in terms of the binding mode revealed in the X-ray crystal structure.
PubMed: 11316871
DOI: 10.1110/ps.48401
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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