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: 19388054 DOI: 10.1002/pro.118 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation