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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 Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855
ChainResidueDetails
AALA226
AASN296
AHIS297

site_idSWS_FT_FI2
Number of Residues5
DetailsSITE: Histone H3K4 binding => ECO:0000269|PubMed:12540855
ChainResidueDetails
ATYR245
AASP256
ATHR266
ALYS317
ATYR335

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

site_idMCSA1
Number of Residues5
DetailsM-CSA 350
ChainResidueDetails
ATYR245activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AHIS293electrostatic stabiliser, hydrogen bond acceptor
AHIS297electrostatic stabiliser, hydrogen bond acceptor
ATYR305activator, electrostatic stabiliser, hydrogen bond acceptor
ATYR335activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-24

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