Structure of PDB 7td5 Chain F

Receptor sequence

>7td5F (length=447) Species: 9606 (Homo sapiens) [Search protein sequence]

SEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQS
MLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETV
LCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMCTPNIDGPNAKSVQ
REQSLHSFHTLFCRRCFKYDCFLHPTGAEESLFRVFHGTYFNNFCSIARL
LGTKTCKQVFQFAVKESLSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEK
FCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWD
CKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGEL
ISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNC
YAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERE

3D structure

PDB

7td5 CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site.

Chain

Resolution

2.994 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

2.1.1.356: [histone H3]-lysine(27) N-trimethyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)
BS01	peptide	F	Q649 A652 D653 D660 L667 F668 N669 V700 Y727 R728 Y729	Q353 A356 D357 D364 L371 F372 N373 V404 Y431 R432 Y433
BS02	peptide	F	D137 I151 E161	D109 I123 E133
BS03	ZN	F	C299 C302 C307 H310	C163 C166 C171 H174
BS04	ZN	F	C454 C465	C195 C206
BS05	ZN	F	C531 C544 C550	C235 C248 C254
BS06	ZN	F	C524 H526 C535	C228 H230 C239
BS07	ZN	F	C524 C537 C544 C548	C228 C241 C248 C252
BS08	ZN	F	C567 C581 C589 C602	C271 C285 C293 C306
BS09	ZN	F	C561 C574 C581 C586	C265 C278 C285 C290
BS10	ZN	F	C561 C563 C567 C572	C265 C267 C271 C276
BS11	SAM	F	A623 G624 W625 M663 S664 S665 F666 N689 H690 Y727 Y737 V738 I740	A327 G328 W329 M367 S368 S369 F370 N393 H394 Y431 Y441 V442 I444

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

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:7td5, PDBe:7td5, PDBj:7td5
PDBsum	7td5
PubMed	36351927
UniProt	Q92800\|EZH1_HUMAN Histone-lysine N-methyltransferase EZH1 (Gene Name=EZH1)

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