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5P78

Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 305

Summary for 5P78
Entry DOI10.2210/pdb5p78/pdb
Group depositionHigh-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits. (G_1002001)
Descriptorendothiapepsin (2 entities in total)
Functional Keywordsfragment screening, method development, aspartic protease, hydrolase
Biological sourceCryphonectria parasitica
Total number of polymer chains1
Total formula weight33813.86
Authors
Schiebel, J.,Heine, A.,Klebe, G. (deposition date: 2016-06-28, release date: 2016-08-03, Last modification date: 2021-11-17)
Primary citationSchiebel, J.,Krimmer, S.G.,Rower, K.,Knorlein, A.,Wang, X.,Park, A.Y.,Stieler, M.,Ehrmann, F.R.,Fu, K.,Radeva, N.,Krug, M.,Huschmann, F.U.,Glockner, S.,Weiss, M.S.,Mueller, U.,Klebe, G.,Heine, A.
High-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits.
Structure, 24:1398-1409, 2016
Cited by
PubMed: 27452405
DOI: 10.1016/j.str.2016.06.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.687 Å)
Structure validation

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