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5E83

CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN S (LIGANDED SICKLE CELL HEMOGLOBIN) COMPLEXED WITH GBT440, CO-CRYSTALLIZATION EXPERIMENT

Summary for 5E83
Entry DOI10.2210/pdb5e83/pdb
DescriptorHemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (8 entities in total)
Functional Keywordsmutant human hemoglobin s[betae6v], r2 quaternary state, oxygen transport
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight65301.92
Authors
Patskovska, L.,Patskovsky, Y.,Bonanno, J.B.,Almo, S.C. (deposition date: 2015-10-13, release date: 2016-07-20, Last modification date: 2023-09-27)
Primary citationOksenberg, D.,Dufu, K.,Patel, M.P.,Chuang, C.,Li, Z.,Xu, Q.,Silva-Garcia, A.,Zhou, C.,Hutchaleelaha, A.,Patskovska, L.,Patskovsky, Y.,Almo, S.C.,Sinha, U.,Metcalf, B.W.,Archer, D.R.
GBT440 increases haemoglobin oxygen affinity, reduces sickling and prolongs RBC half-life in a murine model of sickle cell disease.
Br.J.Haematol., 175:141-153, 2016
Cited by
PubMed: 27378309
DOI: 10.1111/bjh.14214
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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