Structure of PDB 3to6 Chain A Binding Site BS02

Receptor Information
>3to6 Chain A (length=276) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKK
QYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFL
DHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLP
QYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLIT
LLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDI
LDRYNRLKAKKRRTIDPNRLIWKPPV
Ligand information
Ligand IDCMC
InChIInChI=1S/C23H38N7O18P3S/c1-23(2,18(35)21(36)26-4-3-13(31)25-5-6-52-8-14(32)33)9-45-51(42,43)48-50(40,41)44-7-12-17(47-49(37,38)39)16(34)22(46-12)30-11-29-15-19(24)27-10-28-20(15)30/h10-12,16-18,22,34-35H,3-9H2,1-2H3,(H,25,31)(H,26,36)(H,32,33)(H,40,41)(H,42,43)(H2,24,27,28)(H2,37,38,39)/t12-,16-,17-,18+,22-/m1/s1
InChIKeyOBUOSIHPWVNVJN-GRFIIANRSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)CSCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
CACTVS 3.370CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCSCC(O)=O
OpenEye OEToolkits 1.7.2CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCSCC(=O)O)O
OpenEye OEToolkits 1.7.2CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSCC(=O)O)O
CACTVS 3.370CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[C@@H](O)C(=O)NCCC(=O)NCCSCC(O)=O
FormulaC23 H38 N7 O18 P3 S
NameCARBOXYMETHYL COENZYME *A
ChEMBL
DrugBank
ZINCZINC000085534448
PDB chain3to6 Chain B Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3to6 MYST protein acetyltransferase activity requires active site lysine autoacetylation.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		F258 L259 A303 I305 L306 T307 Q312 R313 M314 G315 G317 L341 S342 R421
Binding residue
(residue number reindexed from 1)		F99 L100 A144 I146 L147 T148 Q153 R154 M155 G156 G158 L182 S183 R262
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) C304 E338
Catalytic site (residue number reindexed from 1) C145 E179
Enzyme Commision number 2.3.1.-
2.3.1.48: histone acetyltransferase.
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3to6, PDBe:3to6, PDBj:3to6
PDBsum3to6
PubMed22020126
UniProtQ08649|ESA1_YEAST Histone acetyltransferase ESA1 (Gene Name=ESA1)

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