Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OX3

SETD3 in Complex with an Actin Peptide with His73 Replaced with Lysine

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	6
Details	binding site for residue GOL Y 101

Chain	Residue
A	ASN153
Y	THR77
Y	ASN78
Y	LYS84
Y	HOH204
Y	HOH209

site_id	AC2
Number of Residues	21
Details	binding site for residue SAH A 601

Chain	Residue
A	PHE105
A	PRO179
A	THR252
A	ARG253
A	ASP274
A	MET275
A	CYS276
A	ASN277
A	HIS278
A	TYR312
A	SER324
A	PHE326
A	GOL603
A	HOH749
A	HOH839
A	HOH849
A	HOH850
Y	LYS73
A	ARG74
A	GLU102
A	GLU103

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 602

Chain	Residue
A	LYS125
A	PHE170
A	TRP171
A	HOH778

site_id	AC4
Number of Residues	7
Details	binding site for residue GOL A 603

Chain	Residue
A	GLU103
A	PRO179
A	GLU181
A	TYR182
A	SAH601
A	HOH788
A	HOH799

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 604

Chain	Residue
A	ILE338
A	LYS339
A	ARG432
A	HOH768
A	HOH886

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 605

Chain	Residue
A	TYR287
A	ASN288
A	LEU289
A	GLU290

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO A 606

Chain	Residue
A	LYS448
A	EDO617

site_id	AC8
Number of Residues	10
Details	binding site for residue EDO A 607

Chain	Residue
A	SER316
A	ASN317
A	ALA318
A	ASP334
A	ARG335
A	VAL336
A	LEU466
A	GLU470
A	EDO609
A	EDO612

site_id	AC9
Number of Residues	8
Details	binding site for residue EDO A 608

Chain	Residue
A	ASP204
A	ALA318
A	GLU319
A	ILE322
A	HIS323
A	EDO609
A	EDO612
A	HOH754

site_id	AD1
Number of Residues	9
Details	binding site for residue EDO A 609

Chain	Residue
A	GLN200
A	ALA201
A	ASP204
A	ALA318
A	LYS337
A	GLU470
A	EDO607
A	EDO608
A	EDO612

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO A 610

Chain	Residue
A	ALA382
A	ILE407

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO A 611

Chain	Residue
A	ILE113
A	LYS114
A	ASP301
A	PHE302
A	ARG303
B	LYS114

site_id	AD4
Number of Residues	7
Details	binding site for residue EDO A 612

Chain	Residue
A	SER316
A	ALA318
A	ARG335
A	VAL336
A	EDO607
A	EDO608
A	EDO609

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO A 613

Chain	Residue
A	LEU451
A	HIS454
A	ASP455
A	LEU456
A	LYS461

site_id	AD6
Number of Residues	4
Details	binding site for residue EDO A 614

Chain	Residue
B	HOH720
A	LYS101
B	GLU102
B	PGE614

site_id	AD7
Number of Residues	7
Details	binding site for residue EDO A 615

Chain	Residue
A	GLN256
A	ILE257
A	PRO258
A	VAL265
Y	TYR69
Y	PRO70
Y	ILE71

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO A 616

Chain	Residue
A	ASP334
A	GLU472
A	ILE473
A	HOH718

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO A 617

Chain	Residue
A	GLU472
A	EDO606

site_id	AE1
Number of Residues	6
Details	binding site for residue EDO A 618

Chain	Residue
A	THR69
A	PHE70
A	ASP71
B	LYS64
B	LEU66
B	THR69

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO A 619

Chain	Residue
A	GLU48
A	SER207
A	LYS210
A	HOH831
A	HOH866

site_id	AE3
Number of Residues	5
Details	binding site for residue EDO A 620

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

site_id	AE4
Number of Residues	4
Details	binding site for residue EDO A 621

Chain	Residue
A	GLN63
A	TYR220
A	SER237
A	PHE238

site_id	AE5
Number of Residues	1
Details	binding site for residue EDO A 622

Chain	Residue
A	SER364

site_id	AE6
Number of Residues	6
Details	binding site for residue EDO A 623

Chain	Residue
A	PHE327
A	VAL458
A	LYS461
A	MET462
A	LYS465
A	EDO627

site_id	AE7
Number of Residues	6
Details	binding site for residue EDO A 624

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

site_id	AE8
Number of Residues	8
Details	binding site for residue EDO A 625

Chain	Residue
A	TYR220
A	ILE223
A	GLN224
A	LEU234
A	LYS235
A	SER237
A	HOH835
A	HOH864

site_id	AE9
Number of Residues	5
Details	binding site for residue EDO A 626

Chain	Residue
A	LEU340
A	GLY341
A	PHE387
A	ARG432
A	HOH886

site_id	AF1
Number of Residues	8
Details	binding site for residue EDO A 627

Chain	Residue
A	ASP183
A	GLY325
A	PHE326
A	PHE327
A	VAL458
A	MET462
A	EDO623
A	HOH749

site_id	AF2
Number of Residues	5
Details	binding site for residue ACT A 628

Chain	Residue
A	PHE367
A	ALA368
A	SER377
A	GLN379
A	HOH780

site_id	AF3
Number of Residues	22
Details	binding site for residue SAH B 601

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	PGE614
B	HOH751
B	HOH816
B	HOH827
B	HOH834
B	HOH838
Z	LYS73

site_id	AF4
Number of Residues	5
Details	binding site for residue EDO B 602

Chain	Residue
B	ILE283
B	GLY313
B	THR314
B	HOH716
Z	GLU72

site_id	AF5
Number of Residues	3
Details	binding site for residue EDO B 603

Chain	Residue
B	ALA359
B	ILE407
B	HOH754

site_id	AF6
Number of Residues	4
Details	binding site for residue EDO B 604

Chain	Residue
A	ASP76
B	ARG60
B	LYS61
B	GLN63

site_id	AF7
Number of Residues	4
Details	binding site for residue EDO B 605

Chain	Residue
B	ASP183
B	ARG459
B	EDO610
B	HOH769

site_id	AF8
Number of Residues	4
Details	binding site for residue EDO B 606

Chain	Residue
B	LEU340
B	GLY341
B	PHE387
B	ARG432

site_id	AF9
Number of Residues	3
Details	binding site for residue EDO B 607

Chain	Residue
B	LYS83
B	HOH708
B	HOH709

site_id	AG1
Number of Residues	7
Details	binding site for residue EDO B 608

Chain	Residue
B	ASN317
B	ALA318
B	ASP334
B	ARG335
B	LEU466
B	GLY469
B	GLU470

site_id	AG2
Number of Residues	2
Details	binding site for residue EDO B 609

Chain	Residue
B	HIS333
B	ARG335

site_id	AG3
Number of Residues	5
Details	binding site for residue EDO B 610

Chain	Residue
B	PRO179
B	SER180
B	GLU181
B	EDO605
B	HOH895

site_id	AG4
Number of Residues	4
Details	binding site for residue EDO B 611

Chain	Residue
B	GLN63
B	TYR220
B	SER237
B	PHE238

site_id	AG5
Number of Residues	5
Details	binding site for residue EDO B 612

Chain	Residue
B	HIS397
B	ARG406
B	THR409
B	LEU410
B	PHE415

site_id	AG6
Number of Residues	1
Details	binding site for residue EDO B 613

Chain	Residue
B	ARG293

site_id	AG7
Number of Residues	11
Details	binding site for residue PGE B 614

Chain	Residue
A	EDO614
B	ASP183
B	GLY325
B	PHE326
B	PHE327
B	VAL458
B	LYS461
B	MET462
B	LYS465
B	SAH601
B	HOH769

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	2
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"23673617","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	440
Details	Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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)