6OQA

Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product

Summary for 6OQA

• Entry DOI: 10.2210/pdb6oqa/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase FKBP1A, MALONIC ACID, Centrosome-associated protein CEP250, ... (11 entities in total)
• Functional Keywords: fkbp12, cep250, natural product, ternary complex, cell cycle, isomerase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 8
• Total formula weight: 100330.44

Authors

Lee, S.-J.,Shigdel, U.K.,Townson, S.A.,Verdine, G.L. (deposition date: 2019-04-26, release date: 2020-04-29, Last modification date: 2024-03-13)

• Primary citation: Shigdel, U.K.,Lee, S.J.,Sowa, M.E.,Bowman, B.R.,Robison, K.,Zhou, M.,Pua, K.H.,Stiles, D.T.,Blodgett, J.A.V.,Udwary, D.W.,Rajczewski, A.T.,Mann, A.S.,Mostafavi, S.,Hardy, T.,Arya, S.,Weng, Z.,Stewart, M.,Kenyon, K.,Morgenstern, J.P.,Pan, E.,Gray, D.C.,Pollock, R.M.,Fry, A.M.,Klausner, R.D.,Townson, S.A.,Verdine, G.L.; Genomic discovery of an evolutionarily programmed modality for small-molecule targeting of an intractable protein surface.; Proc.Natl.Acad.Sci.USA, 117:17195-17203, 2020; PubMed: 32606248; DOI: 10.1073/pnas.2006560117

Experimental method

X-RAY DIFFRACTION (2.2 Å)