3FVF
The Crystal Structure of Prostasin Complexed with Camostat at 1.6 Angstroms Resolution
Summary for 3FVF
Entry DOI | 10.2210/pdb3fvf/pdb |
Related | 3E0N 3E0P 3E16 3E1X |
Descriptor | Prostasin, GLYCEROL, 1-[4-(hydroxymethyl)phenyl]guanidine, ... (5 entities in total) |
Functional Keywords | prostasin, hcap-1, channel activating protease, inhibitor, serine protease, enac, cell membrane, glycoprotein, hydrolase, membrane, protease, secreted, 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 | 30021.55 |
Authors | Spraggon, G.,Hornsby, M.,Shipway, A.,Harris, J.L.,Lesley, S.A. (deposition date: 2009-01-15, release date: 2009-05-05, Last modification date: 2021-10-20) |
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 (1.6 Å) |
Structure validation
Download full validation report