4J7I

SET7/9Y335F in complex with TAF10 peptide and AdoHcy

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005694	cellular_component	chromosome
A	0006355	biological_process	regulation of DNA-templated transcription
A	0016279	molecular_function	protein-lysine N-methyltransferase activity
A	0140945	molecular_function	histone H3K4 monomethyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SAH A 800

Chain	Residue
A	ALA226
A	GLU228
A	GLY264
A	ASN265
A	HIS293
A	LYS294
A	ASN296
A	HIS297
A	TRP352

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6,N6,N6-trimethyllysine; alternate => ECO:0000269|PubMed:15099517, ECO:0000269|PubMed:16415881, ECO:0000269|PubMed:25959397

Chain	Residue	Details
B	LYS189
A	ASN296
A	HIS297

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855

Chain	Residue	Details
A	GLU356

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site_id	SWS_FT_FI3
Number of Residues	5
Details	SITE: Histone H3K4 binding => ECO:0000269|PubMed:12540855

Chain	Residue	Details
A	TYR245
A	ASP256
A	THR266
A	LYS317
A	PHE335

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 350

Chain	Residue	Details
A	TYR245	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	HIS293	electrostatic stabiliser, hydrogen bond acceptor
A	HIS297	electrostatic stabiliser, hydrogen bond acceptor
A	TYR305	activator, electrostatic stabiliser, hydrogen bond acceptor
A	PHE335	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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