6OX5

A SETD3 Mutant (N255A) 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	0008170	molecular_function	N-methyltransferase activity
A	0008276	molecular_function	protein methyltransferase activity
A	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
A	0016279	molecular_function	protein-lysine N-methyltransferase 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	0051149	biological_process	positive regulation of muscle cell differentiation
A	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
A	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 SAH A 601

Chain	Residue
A	ARG74
A	HIS278
A	TYR312
A	SER324
A	PHE326
A	EDO602
A	HOH796
A	HOH807
A	HOH822
A	HOH828
Y	LYS73
A	GLU103
A	PHE105
A	PRO179
A	THR252
A	ARG253
A	ASP274
A	MET275
A	ASN277

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site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 602

Chain	Residue
A	GLU103
A	TYR182
A	SAH601

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site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 603

Chain	Residue
A	TYR195
A	ARG467
A	HOH800

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site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 604

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

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site_id	AC5
Number of Residues	8
Details	binding site for residue EDO A 605

Chain	Residue
A	PRO42
A	GLY43
A	LEU399
A	GLY400
A	ASP401
A	SER402
A	ALA403
A	ARG406

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 606

Chain	Residue
A	ASP334
A	GLY469
A	GLU472
A	HOH854

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO A 607

Chain	Residue
A	PHE70
A	ARG164
A	ILE175
A	LEU178
A	SER180
A	HOH757

---

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO A 608

Chain	Residue
A	ASP80
A	LYS83
A	GLU87

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 609

Chain	Residue
A	ARG124
A	THR129
A	GLU131
A	HOH732

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215, ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12, ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT, ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT, ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK, ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0, ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2, ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4, ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62, ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1, ECO:0007744|PDB:6WK2

Chain	Residue	Details
A	ARG74
A	GLU103
A	ARG253
A	ASP274
A	SER324

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER512

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