Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6UJH

Discovery of fragment-inspired heterocyclic benzenesulfonamides as inhibitors of the WDR5-MYC interaction

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000123	cellular_component	histone acetyltransferase complex
A	0001501	biological_process	skeletal system development
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0006094	biological_process	gluconeogenesis
A	0006325	biological_process	chromatin organization
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0035064	molecular_function	methylated histone binding
A	0035097	cellular_component	histone methyltransferase complex
A	0042393	molecular_function	histone binding
A	0042800	molecular_function	histone H3K4 methyltransferase activity
A	0044545	cellular_component	NSL complex
A	0044665	cellular_component	MLL1/2 complex
A	0044666	cellular_component	MLL3/4 complex
A	0045722	biological_process	positive regulation of gluconeogenesis
A	0045815	biological_process	transcription initiation-coupled chromatin remodeling
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0045995	biological_process	regulation of embryonic development
A	0048188	cellular_component	Set1C/COMPASS complex
A	0051302	biological_process	regulation of cell division
A	0051726	biological_process	regulation of cell cycle
A	0071339	cellular_component	MLL1 complex
A	0072686	cellular_component	mitotic spindle
A	0090043	biological_process	regulation of tubulin deacetylation
A	0140672	cellular_component	ATAC complex
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000123	cellular_component	histone acetyltransferase complex
B	0001501	biological_process	skeletal system development
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0006094	biological_process	gluconeogenesis
B	0006325	biological_process	chromatin organization
B	0006355	biological_process	regulation of DNA-templated transcription
B	0006357	biological_process	regulation of transcription by RNA polymerase II
B	0035064	molecular_function	methylated histone binding
B	0035097	cellular_component	histone methyltransferase complex
B	0042393	molecular_function	histone binding
B	0042800	molecular_function	histone H3K4 methyltransferase activity
B	0044545	cellular_component	NSL complex
B	0044665	cellular_component	MLL1/2 complex
B	0044666	cellular_component	MLL3/4 complex
B	0045722	biological_process	positive regulation of gluconeogenesis
B	0045815	biological_process	transcription initiation-coupled chromatin remodeling
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0045995	biological_process	regulation of embryonic development
B	0048188	cellular_component	Set1C/COMPASS complex
B	0051302	biological_process	regulation of cell division
B	0051726	biological_process	regulation of cell cycle
B	0071339	cellular_component	MLL1 complex
B	0072686	cellular_component	mitotic spindle
B	0090043	biological_process	regulation of tubulin deacetylation
B	0140672	cellular_component	ATAC complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue QBS A 401

Chain	Residue
A	PRO224
A	ASN225
A	VAL268
A	LYS272
A	HOH530
A	HOH701
B	TYR75
B	ASP76
B	LYS331

site_id	AC2
Number of Residues	9
Details	binding site for residue SO4 A 402

Chain	Residue
A	LYS123
A	THR124
A	LYS256
A	HOH519
A	HOH529
A	HOH544
A	HOH630
A	HOH664
A	HOH706

site_id	AC3
Number of Residues	11
Details	binding site for residue SO4 A 403

Chain	Residue
A	LYS221
A	ASN265
A	ALA308
A	CYS309
A	HOH514
A	HOH567
A	HOH579
A	HOH648
A	HOH689
A	HOH696
A	HOH724

site_id	AC4
Number of Residues	10
Details	binding site for residue QBS B 401

Chain	Residue
A	TYR75
A	ASP76
A	LYS331
B	PRO224
B	ASN225
B	TYR228
B	VAL268
B	LYS272
B	HOH626
B	HOH698

site_id	AC5
Number of Residues	11
Details	binding site for residue SO4 B 402

Chain	Residue
B	LYS221
B	ASN265
B	ALA308
B	CYS309
B	HOH505
B	HOH538
B	HOH558
B	HOH621
B	HOH641
B	HOH681
B	HOH682

site_id	AC6
Number of Residues	6
Details	binding site for residue DMS B 403

Chain	Residue
B	CYS248
B	LEU249
B	LYS250
B	THR251
B	HOH552
B	HOH622

site_id	AC7
Number of Residues	4
Details	binding site for residue DMS B 404

Chain	Residue
B	TRP95
B	SER97
B	PHE137
B	ASN138

site_id	AC8
Number of Residues	2
Details	binding site for residue DMS B 405

Chain	Residue
B	TYR228
B	GLN289

Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsdDkTLKIWDV

Chain	Residue	Details
A	LEU102-VAL116
A	ILE144-VAL158
A	ILE186-THR200
A	ILE274-LEU288

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	SITE: Important for interaction with histone H3

Chain	Residue	Details
A	ASP107
A	PHE133
A	PHE263
A	GLU322
B	ASP107
B	PHE133
B	PHE263
B	GLU322

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS112
B	LYS112

site_id	SWS_FT_FI3
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS27
A	LYS46
B	LYS27
B	LYS46

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)