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Receptor Information

>3q33 Chain A (length=394) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPNKDDKRVPKSTIKTQ
HFFSLFHQGKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNTRVSV
RDITKIILEFILSIDPNYYLQKVKPAIRSSPELISAASTPARTLRILARR
LKQSGSTVLKEQQDLYLSFTCPREILTKICLFTRPASQYLFPDSSKNSKK
HILNGEELMKWWGFILDRLLIECFQNDTQAKLRIPGEDPARVRSYLRGMK
YPLWQVGDIFTSKENSLAVYNIPLFPDDPKARFIHQLAEEDRLLKVSLSS
FWIELQERQEFKLSVTSSVMGISGYSLATPSLFPSSADVIVPKSRKQFRA
IKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQSLTGKREH

Ligand ID

ACO

InChI

InChI=1S/C23H38N7O17P3S/c1-12(31)51-7-6-25-14(32)4-5-26-21(35)18(34)23(2,3)9-44-50(41,42)47-49(39,40)43-8-13-17(46-48(36,37)38)16(33)22(45-13)30-11-29-15-19(24)27-10-28-20(15)30/h10-11,13,16-18,22,33-34H,4-9H2,1-3H3,(H,25,32)(H,26,35)(H,39,40)(H,41,42)(H2,24,27,28)(H2,36,37,38)/t13-,16-,17-,18+,22-/m1/s1

InChIKey

ZSLZBFCDCINBPY-ZSJPKINUSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(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)O
CACTVS 3.341	CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(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
ACDLabs 10.04	O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C
CACTVS 3.341	CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0	CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O

Formula

C23 H38 N7 O17 P3 S

Name

ACETYL COENZYME *A

PDB chain

3q33 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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Structure summary

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PDB	3q33 Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation.
Resolution	2.8 Å
Binding residue (original residue number in PDB)	A88 T90 V100 R101 F192 P195 A196 Y199 H211 L218 W221 W222
Binding residue (residue number reindexed from 1)	A88 T90 V100 R101 F182 P185 A186 Y189 H201 L208 W211 W212
Annotation score	4

Enzyme Commision number

2.3.1.48: histone acetyltransferase.

	Molecular Function
GO:0004402	histone acetyltransferase activity
GO:0005515	protein binding
GO:0010484	histone H3 acetyltransferase activity
GO:0016740	transferase activity
GO:0032931	histone H3K56 acetyltransferase activity
GO:0036408	histone H3K14 acetyltransferase activity
GO:0043992	histone H3K9 acetyltransferase activity
GO:0043994	histone H3K23 acetyltransferase activity
GO:0044017	histone H3K27 acetyltransferase activity
GO:0061733	peptide-lysine-N-acetyltransferase activity

	Biological Process
GO:0006325	chromatin organization
GO:0006334	nucleosome assembly
GO:0006355	regulation of DNA-templated transcription
GO:0006357	regulation of transcription by RNA polymerase II
GO:0006974	DNA damage response
GO:0010468	regulation of gene expression
GO:0010526	retrotransposon silencing
GO:0033554	cellular response to stress
GO:0036211	protein modification process
GO:0043007	maintenance of rDNA
GO:1990414	replication-born double-strand break repair via sister chromatid exchange
GO:2001032	regulation of double-strand break repair via nonhomologous end joining

	Cellular Component
GO:0000785	chromatin
GO:0005634	nucleus
GO:0070775	H3 histone acetyltransferase complex

PDB	RCSB:3q33, PDBe:3q33, PDBj:3q33
PDBsum	3q33
PubMed	21256037
UniProt	Q07794\|RT109_YEAST Histone acetyltransferase RTT109 (Gene Name=RTT109)

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Structure of PDB 3q33 Chain A Binding Site BS02