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1MUF

Structure of histone H3 K4-specific methyltransferase SET7/9

Functional Information from GO Data
ChainGOidnamespacecontents
A0005694cellular_componentchromosome
A0006355biological_processregulation of DNA-templated transcription
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0140945molecular_functionhistone H3K4 monomethyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsRepeat: {"description":"MORN 3"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12514135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsSite: {"description":"Histone H3K4 binding","evidences":[{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1h3i
ChainResidueDetails
ATYR335
AHIS293

site_idMCSA1
Number of Residues4
DetailsM-CSA 350
ChainResidueDetails
AASN265activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
APHE313electrostatic stabiliser, hydrogen bond acceptor
ALYS317electrostatic stabiliser, hydrogen bond acceptor
AVAL325activator, electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2025-07-09

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