Structure of PDB 1qsm Chain D Binding Site BS01

Receptor Information
>1qsm Chain D (length=152) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEDNITVRFVTENDKEGWQRLWKSYQDFYEVSFPDDLDDFNFGRFLDPNI
KMWAAVAVESSSEKIIGMINFFNHMTTWDFKDKIYINDLYVDENSRVKGA
GGKLIQFVYDEADKLGTPSVYWCTDESNHRAQLLYVKVGYKAPKILYKRK
GY
Ligand information
Ligand IDACO
InChIInChI=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
InChIKeyZSLZBFCDCINBPY-ZSJPKINUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=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 3.341CC(=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 10.04O=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 3.341CC(=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 1.5.0CC(=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
FormulaC23 H38 N7 O17 P3 S
NameACETYL COENZYME *A
ChEMBLCHEMBL1230809
DrugBank
ZINCZINC000008551095
PDB chain1qsm Chain D Residue 1203 [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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PDB1qsm Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		F32 L93 Y94 V95 R100 G103 A104 G105 C127 T128 N132 R134 A135 L137 L138 Y139 K141
Binding residue
(residue number reindexed from 1)		F28 L89 Y90 V91 R96 G99 A100 G101 C123 T124 N128 R130 A131 L133 L134 Y135 K137
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.1.48: histone acetyltransferase.
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
GO:0008080 N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042802 identical protein binding
GO:0061733 peptide-lysine-N-acetyltransferase activity
Biological Process
GO:0006325 chromatin organization
GO:0006338 chromatin remodeling
GO:0032917 polyamine acetylation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:1990331 Hpa2 acetyltransferase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1qsm, PDBe:1qsm, PDBj:1qsm
PDBsum1qsm
PubMed10600387
UniProtQ06592|HPA2_YEAST Histone acetyltransferase HPA2 (Gene Name=HPA2)

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