Structure of PDB 7td5 Chain A

Receptor sequence

>7td5A (length=497) Species: 9606 (Homo sapiens) [Search protein sequence]

SEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQS
MLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETV
LCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEQCTPNIDGPNAKSVQR
EQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDC
FLLLEGAKEYAMLHNVEAPSPVEWTGAEESLFRVFHGTYFNNFCSIARLL
GTKTCKQVFQFAVKESLILSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCE
KFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHW
DCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGE
LISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPN
CYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIER

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	A	T516 Q649 D653 G656 D660 L667 F668 A698 Y727 R728 Y729	T271 Q404 D408 G411 D415 L422 F423 A453 Y482 R483 Y484
BS02	peptide	A	Y134 D137 E161	Y106 D109 E133
BS03	ZN	A	C299 C302 C307 H310	C162 C165 C170 H173
BS04	ZN	A	C337 C454 C465	C200 C244 C255
BS05	ZN	A	C531 C544 C550	C286 C299 C305
BS06	ZN	A	C524 H526 C531 C535	C279 H281 C286 C290
BS07	ZN	A	C524 C537 C544 C548	C279 C292 C299 C303
BS08	ZN	A	C567 C581 C589 C602	C322 C336 C344 C357
BS09	ZN	A	C561 C574 C581 C586	C316 C329 C336 C341
BS10	ZN	A	C561 C563 C567 C572	C316 C318 C322 C327
BS11	SAM	A	A623 G624 W625 S664 S665 F666 N689 H690 Y727 Y737 V738 I740	A378 G379 W380 S419 S420 F421 N444 H445 Y482 Y492 V493 I495

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

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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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