Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OX0

SETD3 in Complex with an Actin Peptide with Sinefungin Replacing SAH as Cofactor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0003713	molecular_function	transcription coactivator activity
A	0003779	molecular_function	actin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0006338	biological_process	chromatin remodeling
A	0008168	molecular_function	methyltransferase activity
A	0016279	molecular_function	protein-lysine N-methyltransferase activity
A	0016740	molecular_function	transferase activity
A	0018021	biological_process	peptidyl-histidine methylation
A	0018023	biological_process	peptidyl-lysine trimethylation
A	0018064	molecular_function	protein-L-histidine N-tele-methyltransferase activity
A	0030047	biological_process	actin modification
A	0032259	biological_process	methylation
A	0042800	molecular_function	histone H3K4 methyltransferase activity
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046975	molecular_function	histone H3K36 methyltransferase activity
A	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
A	0070472	biological_process	regulation of uterine smooth muscle contraction
B	0000785	cellular_component	chromatin
B	0003713	molecular_function	transcription coactivator activity
B	0003779	molecular_function	actin binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0006338	biological_process	chromatin remodeling
B	0008168	molecular_function	methyltransferase activity
B	0016279	molecular_function	protein-lysine N-methyltransferase activity
B	0016740	molecular_function	transferase activity
B	0018021	biological_process	peptidyl-histidine methylation
B	0018023	biological_process	peptidyl-lysine trimethylation
B	0018064	molecular_function	protein-L-histidine N-tele-methyltransferase activity
B	0030047	biological_process	actin modification
B	0032259	biological_process	methylation
B	0042800	molecular_function	histone H3K4 methyltransferase activity
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046975	molecular_function	histone H3K36 methyltransferase activity
B	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
B	0070472	biological_process	regulation of uterine smooth muscle contraction

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue SFG A 1001

Chain	Residue
A	ARG74
A	ASN277
A	HIS278
A	TYR312
A	SER324
A	PHE326
A	HOH1224
A	HOH1242
A	HOH1285
A	HOH1293
Y	HIS73
A	GLU102
A	GLU103
A	PHE105
A	PRO179
A	ARG253
A	ASP274
A	MET275
A	CYS276

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 1002

Chain	Residue
A	LYS448
A	LEU451
A	HOH1172
A	HOH1276

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 1003

Chain	Residue
A	ASP204
A	HIS323
A	EDO1004

site_id	AC4
Number of Residues	8
Details	binding site for residue EDO A 1004

Chain	Residue
A	GLN200
A	ALA201
A	ASP204
A	ALA318
A	LYS337
A	GLU470
A	EDO1003
A	EDO1006

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 1005

Chain	Residue
A	ILE24
A	GLN63
A	TYR220
A	SER237
A	PHE238

site_id	AC6
Number of Residues	8
Details	binding site for residue EDO A 1006

Chain	Residue
A	ASN317
A	ALA318
A	ASP334
A	ARG335
A	VAL336
A	LEU466
A	GLU470
A	EDO1004

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO A 1007

Chain	Residue
A	LEU340
A	GLY341
A	ARG432

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO A 1008

Chain	Residue
A	GLU96
A	MET97
A	HOH1157

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 1009

Chain	Residue
A	PHE327
A	VAL458
A	LYS461
A	LYS465
A	HOH1193
A	HOH1209

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO A 1010

Chain	Residue
A	GLN256
A	ILE257
A	PRO258
A	VAL265
Y	TYR69
Y	PRO70

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO A 1011

Chain	Residue
A	SER198
A	HIS203
A	PHE206
A	HOH1194
A	HOH1257

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO A 1012

Chain	Residue
A	LYS101
A	GLU102
A	VAL458
A	HOH1193
A	HOH1416
B	LYS101

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO A 1013

Chain	Residue
A	PHE367
A	ALA368
A	SER377
A	HOH1120

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO A 1014

Chain	Residue
A	ASP329
A	ASN330

site_id	AD6
Number of Residues	2
Details	binding site for residue EDO A 1015

Chain	Residue
A	TRP121
A	ARG293

site_id	AD7
Number of Residues	1
Details	binding site for residue EDO A 1016

Chain	Residue
A	HOH1150

site_id	AD8
Number of Residues	7
Details	binding site for residue EDO A 1017

Chain	Residue
A	ASP334
A	PHE371
A	GLY469
A	GLU472
A	ILE473
A	HOH1104
A	HOH1116

site_id	AD9
Number of Residues	5
Details	binding site for residue EDO A 1018

Chain	Residue
A	GLN200
A	LYS337
A	ILE338
A	LYS339
A	LEU436

site_id	AE1
Number of Residues	6
Details	binding site for residue EDO A 1019

Chain	Residue
A	ASP401
A	SER402
A	ALA403
A	ARG406
A	LEU399
A	GLY400

site_id	AE2
Number of Residues	22
Details	binding site for residue SFG B 1001

Chain	Residue
B	ARG74
B	GLU102
B	GLU103
B	PHE105
B	PRO179
B	THR252
B	ARG253
B	ASP274
B	MET275
B	CYS276
B	ASN277
B	HIS278
B	TYR312
B	SER324
B	PHE326
B	HOH1196
B	HOH1212
B	HOH1266
B	HOH1294
B	HOH1304
B	HOH1311
Z	HIS73

site_id	AE3
Number of Residues	2
Details	binding site for residue EDO B 1002

Chain	Residue
B	ALA359
B	ILE407

site_id	AE4
Number of Residues	3
Details	binding site for residue EDO B 1003

Chain	Residue
B	TYR182
B	ASP183
B	HOH1222

site_id	AE5
Number of Residues	5
Details	binding site for residue EDO B 1004

Chain	Residue
B	LEU340
B	GLY341
B	PHE387
B	ARG432
B	HOH1109

site_id	AE6
Number of Residues	3
Details	binding site for residue EDO B 1005

Chain	Residue
B	HIS333
B	ARG335
B	HIS370

site_id	AE7
Number of Residues	2
Details	binding site for residue EDO B 1006

Chain	Residue
B	ASP191
B	ASP291

site_id	AE8
Number of Residues	6
Details	binding site for residue EDO B 1007

Chain	Residue
B	LEU282
B	THR284
B	THR285
B	ILE310
B	PHE311
Z	HOH103

site_id	AE9
Number of Residues	6
Details	binding site for residue EDO B 1008

Chain	Residue
B	THR314
B	ARG315
B	GLU319
B	ARG335
Z	VAL76
Z	HOH105

site_id	AF1
Number of Residues	4
Details	binding site for residue EDO B 1009

Chain	Residue
B	PRO40
B	GLU48
B	SER207
B	LYS210

site_id	AF2
Number of Residues	5
Details	binding site for residue EDO B 1010

Chain	Residue
B	ASP329
B	VAL458
B	LYS461
B	MET462
B	LYS465

site_id	AF3
Number of Residues	6
Details	binding site for residue EDO B 1011

Chain	Residue
A	GLY72
A	ASP76
B	ARG60
B	LYS61
B	GLN63
B	HOH1182

site_id	AF4
Number of Residues	3
Details	binding site for residue EDO B 1012

Chain	Residue
B	ASP334
B	GLU472
B	HOH1219

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"30526847","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30785395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31388018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32503840","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	440
Details	Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30785395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31388018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31911441","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31993215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32503840","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human SET domain-containing protein 3.","authors":["Zeng H.","Dong A.","Walker J.R.","Loppnau P.","Bountra C.","Weigelt J.","Arrowsmith C.H.","Edwards A.M.","Min J.","Wu H."]}},{"source":"PDB","id":"3SMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ICT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ICV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V62","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WK2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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