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-Structure paper
Title | Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. |
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Journal, issue, pages | Protein Sci., Vol. 18, Page 1081-1094, Year 2009 |
Publish date | Jul 31, 2008 (structure data deposition date) |
Authors | Spraggon, G. / Hornsby, M. / Shipway, A. / Tully, D.C. / Bursulaya, B. / Danahay, H. / Harris, J.L. / Lesley, S.A. |
External links | Protein Sci. / PubMed:19388054 |
Methods | X-ray diffraction |
Resolution | 1.3 - 2.8 Å |
Structure data | PDB-3e0n: PDB-3e1x: PDB-3fvf: PDB-3gyl: PDB-3gym: |
Chemicals | ChemComp-SO4: ChemComp-GOL: ChemComp-HOH: ChemComp-1JZ: ChemComp-DMS: ChemComp-CA: |
Source |
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Keywords | HYDROLASE / PROSTASIN / PROTEASE / chloromethyl-ketone / Channel / ENaC / Cell membrane / Glycoprotein / Membrane / Secreted / Serine protease / Transmembrane / Zymogen / HCAP-1 / Channel Activating Protease / INHIBITOR / DIVALENT CATION / CHANNEL ACTIVATING / Disulfide bond / HYDROLASE/INHIBITOR / hCAP1 / Aprotinin / inhibition / Pharmaceutical / Protease inhibitor / Serine protease inhibitor / HYDROLASE-INHIBITOR COMPLEX |