crystal structure of BCL-2 G101V mutation with venetoclax

Summary for 6O0L

DescriptorApoptosis regulator Bcl-2,Bcl-2-like protein 1,Apoptosis regulator Bcl-2, 4-[4-[[2-(4-chlorophenyl)-4,4-dimethyl-cyclohexen-1-yl]methyl]piperazin-1-yl]-~{N}-[4-(oxan-4-ylmethylamino)-3-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]phenyl]sulfonyl-2-(1~{H}-pyrrolo[2,3-b]pyridin-5-yloxy)benzamide, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordsbcl-2, venetoclax, complex, protein-protein interface inhibitor, resistance mutation, fda approved drug complex, apoptosis
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total molecular weight41033.55
Birkinshaw, R.W.,Luo, C.S.,Colman, P.M.,Czabotar, P.E. (deposition date: 2019-02-16, 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

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.22880 0.8% 3.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution