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3VV0

Crystal structure of histone methyltransferase SET7/9 in complex with DAAM-3

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 Residues17
DetailsBINDING SITE FOR RESIDUE KH3 A 401
ChainResidue
AILE223
ALYS294
AASN296
AHIS297
ATYR305
ATYR335
ATRP352
AGLU356
AHOH606
AALA226
AGLU228
ATYR245
AGLY264
AASN265
ATHR266
ALEU267
AHIS293

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 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_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 2024-10-30

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