4RTD
Escherichia coli alpha-2-macroglobulin activated by porcine elastase
Summary for 4RTD
Entry DOI | 10.2210/pdb4rtd/pdb |
Related | 4ACQ 4U48 4U59 |
Descriptor | Uncharacterized lipoprotein YfhM (1 entity in total) |
Functional Keywords | thioester domain, macroglobulin, lipid binding protein |
Biological source | Escherichia coli |
Cellular location | Cell membrane ; Lipid-anchor : P76578 |
Total number of polymer chains | 1 |
Total formula weight | 181618.08 |
Authors | 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 Cited by PubMed: 26143919DOI: 10.1107/S1399004715008548 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.65 Å) |
Structure validation
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