Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/L133P/L151C/G154A) with matrix metalloproteinase-3 catalytic domain (MMP-3cd)

Summary for 6N9D

DescriptorStromelysin-1, Metalloproteinase inhibitor 1, CALCIUM ION, ... (5 entities in total)
Functional Keywordstissue inhibitor of metalloproteinases, matrix metalloproteinase, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total molecular weight39511.44
Raeeszadeh-Sarmazdeh, M.,Radisky, E.S.,Sankaran, B. (deposition date: 2018-12-03, release date: 2019-05-15, Last modification date: 2019-12-04)
Primary citation
Raeeszadeh-Sarmazdeh, M.,Greene, K.A.,Sankaran, B.,Downey, G.P.,Radisky, D.C.,Radisky, E.S.
Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.
J.Biol.Chem., 294:9476-9488, 2019
PubMed: 31040180 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.RA119.008321
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.2638 0.3% 2.5% 1.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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