Structure of PDB 7td5 Chain A Binding Site BS11

Receptor Information
>7td5 Chain A (length=497) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQS
MLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETV
LCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEQCTPNIDGPNAKSVQR
EQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDC
FLLLEGAKEYAMLHNVEAPSPVEWTGAEESLFRVFHGTYFNNFCSIARLL
GTKTCKQVFQFAVKESLILSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCE
KFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHW
DCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGE
LISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPN
CYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIER
Ligand information
Ligand IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain7td5 Chain A Residue 1009 [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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PDB7td5 CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site.
Resolution2.994 Å
Binding residue
(original residue number in PDB)		A623 G624 W625 S664 S665 F666 N689 H690 Y727 Y737 V738 I740
Binding residue
(residue number reindexed from 1)		A378 G379 W380 S419 S420 F421 N444 H445 Y482 Y492 V493 I495
Annotation score5
Enzymatic activity
Enzyme Commision number 2.1.1.356: [histone H3]-lysine(27) N-trimethyltransferase.
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003682 chromatin binding
GO:0003714 transcription corepressor activity
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0031491 nucleosome binding
GO:0042054 histone methyltransferase activity
GO:0042393 histone binding
GO:0046976 histone H3K27 methyltransferase activity
GO:0140693 molecular condensate scaffold activity
GO:0140951 histone H3K27 trimethyltransferase activity
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0006325 chromatin organization
GO:0006338 chromatin remodeling
GO:0009653 anatomical structure morphogenesis
GO:0021766 hippocampus development
GO:0031507 heterochromatin formation
GO:0031509 subtelomeric heterochromatin formation
GO:0032259 methylation
GO:0045944 positive regulation of transcription by RNA polymerase II
Cellular Component
GO:0000781 chromosome, telomeric region
GO:0000792 heterochromatin
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0035098 ESC/E(Z) complex

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7td5, PDBe:7td5, PDBj:7td5
PDBsum7td5
PubMed36351927
UniProtQ92800|EZH1_HUMAN Histone-lysine N-methyltransferase EZH1 (Gene Name=EZH1)

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