1N6A

Structure of SET7/9

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	19
Details	BINDING SITE FOR RESIDUE SAM A 402

Chain	Residue
A	ALA226
A	TYR335
A	TRP352
A	GLU356
A	HOH1030
A	HOH1118
A	HOH1130
A	HOH1153
A	HOH1159
A	HOH1161
A	HOH1219
A	GLU228
A	GLY264
A	ASN265
A	HIS293
A	LYS294
A	ALA295
A	ASN296
A	HIS297

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12514135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Site: {"description":"Histone H3K4 binding","evidences":[{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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	ASN265	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	PHE313	electrostatic stabiliser, hydrogen bond acceptor
A	LYS317	electrostatic stabiliser, hydrogen bond acceptor
A	VAL325	activator, electrostatic stabiliser, hydrogen bond acceptor
A	ALA359	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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