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2RFI

Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and dimethylated H3K9 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0002039molecular_functionp53 binding
A0005634cellular_componentnucleus
A0008270molecular_functionzinc ion binding
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0042054molecular_functionhistone methyltransferase activity
A0046974molecular_functionhistone H3K9 methyltransferase activity
B0002039molecular_functionp53 binding
B0005634cellular_componentnucleus
B0008270molecular_functionzinc ion binding
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0042054molecular_functionhistone methyltransferase activity
B0046974molecular_functionhistone H3K9 methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS1031
ACYS1044
ACYS1074
ACYS1078

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS1037
ACYS1074
ACYS1080
ACYS1084

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
ACYS1033
ACYS1037
ACYS1042
ACYS1031

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
ACYS1172
ACYS1225
ACYS1227
ACYS1232

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BCYS1031
BCYS1044
BCYS1074
BCYS1078

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS1037
BCYS1074
BCYS1080
BCYS1084

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BCYS1031
BCYS1033
BCYS1037
BCYS1042

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BCYS1172
BCYS1225
BCYS1227
BCYS1232

site_idAC9
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 101
ChainResidue
AMET1105
ATRP1107
ASER1141
ATYR1142
AARG1166
APHE1167
AASN1169
AHIS1170
ATYR1211
APHE1215
APHE1223
ACYS1225
AARG1226
AHOH1322
AHOH1357
AHOH1390
AHOH1446
AHOH1460
AHOH1462
AHOH1472
PMLY7

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SAH A 102
ChainResidue
AHOH1517
BMET1105
BTRP1107
BARG1166
BASN1169
BHIS1170
BTYR1211
BPHE1223
BSER1224
BCYS1225
BARG1226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues126
DetailsDomain: {"description":"Pre-SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00157","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues117
DetailsDomain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues25
DetailsRegion: {"description":"Interaction with histone H3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Histone H3K9me binding","evidences":[{"source":"PubMed","id":"18264113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20084102","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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