Structure of PDB 1mjb Chain A Binding Site BS01

Receptor Information
>1mjb Chain A (length=273) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQY
ERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDH
KTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQY
QRMGYGKLLIEFSYELSKKENKVGSPQKPLSDLGLLSYRAYWSDTLITLL
VEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILD
RYNRLKAKKRRTIDPNRLIWKPP
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 chain1mjb Chain A Residue 500 [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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PDB1mjb The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		W180 F258 L259 A303 C304 L306 T307 Q312 R313 M314 G315 S342 L344 G345 R421
Binding residue
(residue number reindexed from 1)		W19 F97 L98 A142 C143 L145 T146 Q151 R152 M153 G154 S181 L183 G184 R260
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) C304 Q338
Catalytic site (residue number reindexed from 1) C143 Q177
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1mjb, PDBe:1mjb, PDBj:1mjb
PDBsum1mjb
PubMed12368900
UniProtQ08649|ESA1_YEAST Histone acetyltransferase ESA1 (Gene Name=ESA1)

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