3E0N
The X-ray structure of Human Prostasin in complex with DFFR-chloromethyl ketone inhibitor
Summary for 3E0N
| Entry DOI | 10.2210/pdb3e0n/pdb |
| Related | 3E0P 3E16 3E1X |
| Related PRD ID | PRD_002526 |
| Descriptor | Prostasin heavy chain, DPN-PHE-ARM, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | prostasin, protease, chloromethyl-ketone, channel, enac, cell membrane, glycoprotein, hydrolase, membrane, secreted, serine protease, transmembrane, zymogen |
| Biological source | Homo sapiens (human) More |
| 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 | 2 |
| Total formula weight | 30542.99 |
| Authors | Spraggon, G.,Hornsby, M.,Shipway, A.,Harris, J.L.,Lesley, S.A. (deposition date: 2008-07-31, release date: 2009-06-16, Last modification date: 2023-09-20) |
| 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 (1.7 Å) |
Structure validation
Download full validation report
