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3GYM

Structure of Prostasin in Complex with Aprotinin

Summary for 3GYM
Entry DOI10.2210/pdb3gym/pdb
Related3E1X 3EON 3FVF 3GYL
DescriptorProstasin, Pancreatic trypsin inhibitor (2 entities in total)
Functional Keywordsprostasin, 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 sourceHomo sapiens (Human)
More
Cellular locationProstasin: 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 chains4
Total formula weight69508.24
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 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 (2.8 Å)
Structure validation

217705

건을2024-03-27부터공개중

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