1MT6

Structure of histone H3 K4-specific methyltransferase SET7/9 with 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	13
Details	BINDING SITE FOR RESIDUE SAH A 1

Chain	Residue
A	ALA226
A	HOH416
A	HOH447
A	HOH478
A	HOH493
A	GLU228
A	ASN265
A	HIS293
A	LYS294
A	ALA295
A	ASN296
A	HIS297
A	TYR335

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855

Chain	Residue	Details
A	ALA226
A	ASN296
A	HIS297

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site_id	SWS_FT_FI2
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	TYR335

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1h3i

Chain	Residue	Details
A	TYR335
A	HIS293

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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	TYR335	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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