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3E1X

The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution

Summary for 3E1X
Entry DOI10.2210/pdb3e1x/pdb
Related1EON 1EOP 3E16
DescriptorProstasin, GLYCEROL (3 entities in total)
Functional Keywordsprostasin, enac, hcap-1, channel activating protease, cell membrane, glycoprotein, hydrolase, membrane, protease, secreted, serine protease, transmembrane, zymogen
Biological sourceHomo sapiens (human)
Cellular locationProstasin: Cell membrane; Single-pass membrane protein. Prostasin light chain: Secreted, extracellular space. Prostasin heavy chain: Secreted, extracellular space: Q16651
Total number of polymer chains1
Total formula weight29792.19
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 citationSpraggon, 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 (1.7 Å)
Structure validation

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