6O0O

crystal structure of BCL-2 G101V mutation with S55746

Summary for 6O0O

DescriptorApoptosis regulator Bcl-2,Bcl-2-like protein 1,Apoptosis regulator Bcl-2, ~{N}-(4-hydroxyphenyl)-3-[6-[[(3~{S})-3-(morpholin-4-ylmethyl)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]-1,3-benzodioxol-5-yl]-~{N}-phenyl-5,6,7,8-tetrahydroindolizine-1-carboxamide (3 entities in total)
Functional Keywordsbcl-2, s55746, complex, protein-protein interface inhibitor, resistance mutation, apoptosis
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total molecular weight40220.91
Authors
Birkinshaw, R.W.,Luo, C.S.,Colman, P.M.,Czabotar, P.E. (deposition date: 2019-02-17, release date: 2019-05-22, Last modification date: 2019-07-10)
Primary citation
Birkinshaw, R.W.,Gong, J.N.,Luo, C.S.,Lio, D.,White, C.A.,Anderson, M.A.,Blombery, P.,Lessene, G.,Majewski, I.J.,Thijssen, R.,Roberts, A.W.,Huang, D.C.S.,Colman, P.M.,Czabotar, P.E.
Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations.
Nat Commun, 10:2385-2385, 2019
PubMed: 31160589 (PDB entries with the same primary citation)
DOI: 10.1038/s41467-019-10363-1
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.998 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.26740 0.4% 4.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution