Crystal structure of full-length human MMP-12

Summary for 3BA0

DescriptorMacrophage metalloelastase, ZINC ION, CALCIUM ION, ... (5 entities in total)
Functional Keywordsfull-length mmp-12, hemopexin domain, catalytic domain, domain interaction., calcium, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total molecular weight42509.55
Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Myonas, E.,Svergun, D.I. (deposition date: 2007-11-07, release date: 2008-07-29, Last modification date: 2018-07-18)
Primary citation
Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Mylonas, E.,Svergun, D.I.
Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12.
J.Am.Chem.Soc., 130:7011-7021, 2008
PubMed: 18465858 (PDB entries with the same primary citation)
DOI: 10.1021/ja710491y
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.32378 14.3% 30.5% 0.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-10-21