6MBL

SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, Second P212121 Crystal Form

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 1001

Chain	Residue
A	ARG74
A	ASN277
A	HIS278
A	TYR312
A	SER324
A	PHE326
A	EDO1005
A	HOH1135
A	HOH1176
A	HOH1202
Y	HIS73
A	GLU102
A	GLU103
A	PHE105
A	THR252
A	ARG253
A	ASP274
A	MET275
A	CYS276

---

site_id	AC2
Number of Residues	7
Details	binding site for residue EDO A 1002

Chain	Residue
A	PRO40
A	GLU45
A	GLU48
A	HIS203
A	SER207
A	EDO1003
A	HOH1153

---

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO A 1003

Chain	Residue
A	SER207
A	LYS210
A	ASN211
A	ARG214
A	EDO1002

---

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 1004

Chain	Residue
A	PHE70
A	ARG164
A	ILE175
A	LEU178
A	SER180
A	HOH1138

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 1005

Chain	Residue
A	GLU103
A	SAH1001
A	HOH1103

---

site_id	AC6
Number of Residues	3
Details	binding site for residue EDO A 1006

Chain	Residue
A	THR443
A	ILE444
A	HOH1129

---

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 1007

Chain	Residue
A	ASP80
A	LYS83
A	TRP84
A	GLU87

---

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO A 1008

Chain	Residue
A	LEU340
A	GLY341
A	PHE408
A	ARG432
A	EDO1010

---

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO A 1009

Chain	Residue
A	ALA90
A	SER91
A	VAL92
A	GLU93
A	TRP121

---

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

Chain	Residue
A	LYS339
A	ILE404
A	ASP405
A	PHE408
A	ARG432
A	EDO1008

---

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

Chain	Residue
A	ASP334
A	PHE371
A	GLU472
A	ILE473
A	HOH1168

---

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

---

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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