Structure of PDB 1qsm Chain B Binding Site BS01

Receptor Information
>1qsm Chain B (length=149) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NITVRFVTENDKEGWQRLWKSYQDFYEVSFPDDLDDFNFGRFLDPNIKMW
AAVAVESSSEKIIGMINFFNHMTTWDFKDKIYINDLYVDENSRVKGAGGK
LIQFVYDEADKLGTPSVYWCTDESNHRAQLLYVKVGYKAPKILYKRKGY
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 B Residue 1201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
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)		Y33 L93 Y94 V95 R100 V101 G103 A104 G105 C127 T128 N132 R134 A135 Y139 K141
Binding residue
(residue number reindexed from 1)		Y26 L86 Y87 V88 R93 V94 G96 A97 G98 C120 T121 N125 R127 A128 Y132 K134
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)

[Back to BioLiP]