Structure of PDB 4er5 Chain A Binding Site BS01

Receptor Information
>4er5 Chain A (length=329) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKL
AMEYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRH
ILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLF
VDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWY
GKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFAN
MKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSKPVSY
YLHTIDRTILENYFSSLKNPKLREEQEAA
Ligand information
Ligand ID0QK
InChIInChI=1S/C28H41N7O4/c1-17(2)34(13-6-12-30-27(38)33-19-9-7-18(8-10-19)28(3,4)5)15-21-22(36)23(37)26(39-21)35-14-11-20-24(29)31-16-32-25(20)35/h7-11,14,16-17,21-23,26,36-37H,6,12-13,15H2,1-5H3,(H2,29,31,32)(H2,30,33,38)/t21-,22-,23-,26-/m1/s1
InChIKeyWXRGFPHDRFQODR-ICLZECGLSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6CC(C)N(CCCNC(=O)Nc1ccc(cc1)C(C)(C)C)CC2C(C(C(O2)n3ccc4c3ncnc4N)O)O
OpenEye OEToolkits 1.7.6CC(C)N(CCCNC(=O)Nc1ccc(cc1)C(C)(C)C)C[C@@H]2[C@H]([C@H]([C@@H](O2)n3ccc4c3ncnc4N)O)O
CACTVS 3.370CC(C)N(CCCNC(=O)Nc1ccc(cc1)C(C)(C)C)C[CH]2O[CH]([CH](O)[CH]2O)n3ccc4c(N)ncnc34
CACTVS 3.370CC(C)N(CCCNC(=O)Nc1ccc(cc1)C(C)(C)C)C[C@H]2O[C@H]([C@H](O)[C@@H]2O)n3ccc4c(N)ncnc34
ACDLabs 12.01O=C(Nc1ccc(cc1)C(C)(C)C)NCCCN(C(C)C)CC4OC(n3ccc2c(ncnc23)N)C(O)C4O
FormulaC28 H41 N7 O4
Name7-{5-[(3-{[(4-tert-butylphenyl)carbamoyl]amino}propyl)(propan-2-yl)amino]-5-deoxy-beta-D-ribofuranosyl}-7H-pyrrolo[2,3-d]pyrimidin-4-amine
ChEMBLCHEMBL2169919
DrugBank
ZINCZINC000089469833
PDB chain4er5 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4er5 Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors.
Resolution2.57 Å
Binding residue
(original residue number in PDB)		Y128 D161 G163 S164 G165 V169 E186 K187 D222 F223 F239 V240 N241 F245 S268
Binding residue
(residue number reindexed from 1)		Y119 D152 G154 S155 G156 V160 E177 K178 D213 F214 F230 V231 N232 F236 S259
Annotation score1
Binding affinityBindingDB: Ki=0.300000nM,IC50=0.400000nM,EC50=9.0nM,Kd=0.250000nM
Enzymatic activity
Enzyme Commision number 2.1.1.360: [histone H3]-lysine(79) N-trimethyltransferase.
Gene Ontology
Molecular Function
GO:0031151 histone H3K79 methyltransferase activity
Biological Process
GO:0051726 regulation of cell cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:4er5, PDBe:4er5, PDBj:4er5
PDBsum4er5
PubMed23250418
UniProtQ8TEK3|DOT1L_HUMAN Histone-lysine N-methyltransferase, H3 lysine-79 specific (Gene Name=DOT1L)

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