Structure of PDB 4psx Chain D Binding Site BS01

Receptor Information
>4psx Chain D (length=313) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHL
AFDSVTFKPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVD
CFAEERKTHNLSDVFEKVSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIF
SLLFIEAANYIDETDPSWQIYWLLNKKTKELIGFVTTYKYWHYLGAKSFD
EDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAIIQSWLEDKSITEITVED
PNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSLKLEERQ
FNRLVEMLLLLNN
Ligand information
Ligand IDCOA
InChIInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
InChIKeyRGJOEKWQDUBAIZ-IBOSZNHHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(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)NCCS
OpenEye OEToolkits 1.5.0CC(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)NCCS)O
CACTVS 3.341CC(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)NCCS
ACDLabs 10.04O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC21 H36 N7 O16 P3 S
NameCOENZYME A
ChEMBLCHEMBL1213327
DrugBankDB01992
ZINCZINC000008551087
PDB chain4psx Chain D Residue 401 [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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PDB4psx Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex
Resolution2.509 Å
Binding residue
(original residue number in PDB)		I161 F220 L221 I222 Q227 N228 G230 G232 S233 N258 L264 R267
Binding residue
(residue number reindexed from 1)		I155 F214 L215 I216 Q221 N222 G224 G226 S227 N252 L258 R261
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) F220 E255
Catalytic site (residue number reindexed from 1) F214 E249
Enzyme Commision number 2.3.1.48: histone acetyltransferase.
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042393 histone binding
Biological Process
GO:0006325 chromatin organization
GO:0031509 subtelomeric heterochromatin formation
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4psx, PDBe:4psx, PDBj:4psx
PDBsum4psx
PubMed24835250
UniProtQ12341|HAT1_YEAST Histone acetyltransferase type B catalytic subunit (Gene Name=HAT1)

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