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2F69

Ternary complex of SET7/9 bound to AdoHcy and a TAF10 peptide

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 PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 800
ChainResidue
AALA226
ATRP352
AGLU356
AHOH819
AHOH828
AHOH862
AHOH930
AHOH936
AHOH977
AHOH991
AHOH1017
AGLU228
AHOH1142
BMLZ189
AGLY264
AASN265
AHIS293
ALYS294
AASN296
AHIS297
ATYR335

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; alternate => ECO:0000269|PubMed:15099517, ECO:0000269|PubMed:16415881, ECO:0000269|PubMed:25959397
ChainResidueDetails
BMLZ189
AASN296
AHIS297

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855
ChainResidueDetails
AGLU356

site_idSWS_FT_FI3
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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