Escherichia coli alpha-2-macroglobulin activated by porcine elastase

Summary for 4RTD

Related4U48 4U59 4ACQ
DescriptorUncharacterized lipoprotein YfhM (1 entity in total)
Functional Keywordsthioester domain, macroglobulin, lipid binding protein
Biological sourceEscherichia coli
Cellular locationCell membrane ; Lipid-anchor  P76578
Total number of polymer chains1
Total molecular weight181618.08
Fyfe, C.D.,Grinter, R.,Roszak, A.W.,Josts, I.,Cogdell, R.J.,Walker, D. (deposition date: 2014-11-14, release date: 2015-07-15, Last modification date: 2015-07-29)
Primary citation
Fyfe, C.D.,Grinter, R.,Josts, I.,Mosbahi, K.,Roszak, A.W.,Cogdell, R.J.,Wall, D.M.,Burchmore, R.J.,Byron, O.,Walker, D.
Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
Acta Crystallogr.,Sect.D, 71:1478-1486, 2015
PubMed: 26143919 (PDB entries with the same primary citation)
DOI: 10.1107/S1399004715008548
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.239211.6%2.7%2.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-08-12