3GYM
Structure of Prostasin in Complex with Aprotinin
Summary for 3GYM
Entry DOI | 10.2210/pdb3gym/pdb |
Related | 3E1X 3EON 3FVF 3GYL |
Descriptor | Prostasin, Pancreatic trypsin inhibitor (2 entities in total) |
Functional Keywords | prostasin, hcap1, channel activating, aprotinin, inhibition, disulfide bond, pharmaceutical, protease inhibitor, secreted, serine protease inhibitor, cell membrane, glycoprotein, hydrolase, membrane, protease, serine protease, transmembrane, zymogen, hydrolase-inhibitor complex, hydrolase/inhibitor |
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 Secreted: P00974 |
Total number of polymer chains | 4 |
Total formula weight | 69508.24 |
Authors | Spraggon, G.,Hornsby, M.,Shipway, A.,Harris, J.L.,Lesley, S.A. (deposition date: 2009-04-03, release date: 2009-05-05, Last modification date: 2023-09-06) |
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 (2.8 Å) |
Structure validation
Download full validation report