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3HNA

Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and mono-Methylated 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 Residues22
DetailsBINDING SITE FOR RESIDUE SAH A 101
ChainResidue
AHOH120
ASER1141
ATYR1142
AARG1166
APHE1167
AASN1169
AHIS1170
ATYR1211
APHE1215
APHE1223
ASER1224
AHOH173
ACYS1225
AARG1226
PMLZ9
AHOH284
AHOH309
AHOH335
AHOH345
AHOH645
AMET1105
ATRP1107

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS1031
ACYS1044
ACYS1074
ACYS1078

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS1037
ACYS1074
ACYS1080
ACYS1084

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
ACYS1031
ACYS1033
ACYS1037
ACYS1042

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
ACYS1172
ACYS1225
ACYS1227
ACYS1232

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH B 102
ChainResidue
BHOH156
BHOH230
BHOH283
BHOH344
BHOH355
BHOH432
BHOH450
BMET1105
BTRP1107
BSER1141
BTYR1142
BARG1166
BASN1169
BHIS1170
BTYR1211
BPHE1215
BPHE1223
BCYS1225
BARG1226
QMLZ9

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BCYS1031
BCYS1044
BCYS1074
BCYS1078

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS1037
BCYS1074
BCYS1080
BCYS1084

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BCYS1031
BCYS1033
BCYS1037
BCYS1042

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BCYS1172
BCYS1225
BCYS1227
BCYS1232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsBINDING:
ChainResidueDetails
AGLU1062
AVAL1136
AGLU1173
ALEU1200
AALA1203
BGLU1062
BASN1064
BPRO1068
BGLU1073
BASN1075
BMET1105
AASN1064
BVAL1109
BSER1111
BILE1115
BVAL1136
BGLU1173
BLEU1200
BALA1203
APRO1068
AGLU1073
AASN1075
AMET1105
AVAL1109
ASER1111
AILE1115

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Histone H3K9me binding => ECO:0000269|PubMed:18264113, ECO:0000269|PubMed:20084102
ChainResidueDetails
ACYS1155
BCYS1155

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO1004
ASER1048
BPRO1004
BSER1048

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PDB entries from 2024-05-01

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