3E1X
The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution
Summary for 3E1X
Entry DOI | 10.2210/pdb3e1x/pdb |
Related | 1EON 1EOP 3E16 |
Descriptor | Prostasin, GLYCEROL (3 entities in total) |
Functional Keywords | prostasin, enac, hcap-1, channel activating protease, cell membrane, glycoprotein, hydrolase, membrane, protease, secreted, serine protease, transmembrane, zymogen |
Biological source | Homo sapiens (human) |
Cellular location | Prostasin: Cell membrane; Single-pass membrane protein. Prostasin light chain: Secreted, extracellular space. Prostasin heavy chain: Secreted, extracellular space: Q16651 |
Total number of polymer chains | 1 |
Total formula weight | 29792.19 |
Authors | Spraggon, G.,Hornsby, M.,Shipway, A.,Harris, J.L.,Lesley, S.A. (deposition date: 2008-08-04, release date: 2009-05-05, Last modification date: 2023-08-30) |
Primary citation | Spraggon, G.,Hornsby, M.,Shipway, A.,Tully, D.C.,Bursulaya, B.,Danahay, H.,Harris, J.L.,Lesley, S.A. Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. Protein Sci., 18:1081-1094, 2009 Cited by PubMed: 19388054DOI: 10.1002/pro.118 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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