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3MO2

human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67

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
C0002039molecular_functionp53 binding
C0005634cellular_componentnucleus
C0008270molecular_functionzinc ion binding
C0016279molecular_functionprotein-lysine N-methyltransferase activity
C0042054molecular_functionhistone methyltransferase activity
C0046974molecular_functionhistone H3K9 methyltransferase activity
D0002039molecular_functionp53 binding
D0005634cellular_componentnucleus
D0008270molecular_functionzinc ion binding
D0016279molecular_functionprotein-lysine N-methyltransferase activity
D0042054molecular_functionhistone methyltransferase activity
D0046974molecular_functionhistone H3K9 methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 340
ChainResidue
AZN341
AZN342
ACYS1031
ACYS1044
ACYS1074
ACYS1078

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 341
ChainResidue
ACYS1074
ACYS1080
ACYS1084
AZN340
AZN342
ACYS1037

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 342
ChainResidue
AZN340
AZN341
ACYS1031
ACYS1033
ACYS1037
ACYS1042

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 343
ChainResidue
ACYS1172
ACYS1225
ACYS1227
ACYS1232

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE E67 A 1
ChainResidue
AHOH164
AASP1131
AALA1134
AASP1135
AARG1137
AGLU1138
AASP1140
ASER1141
ALEU1143
AASP1145
ATYR1211
AARG1214
APHE1215

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 5
ChainResidue
BZN7
BCYS1031
BCYS1044
BCYS1074
BCYS1078

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 6
ChainResidue
BCYS1037
BCYS1074
BCYS1080
BCYS1084

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 7
ChainResidue
BZN5
BCYS1031
BCYS1033
BCYS1037
BCYS1042

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 8
ChainResidue
BCYS1172
BCYS1225
BCYS1227
BCYS1232

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE E67 B 2
ChainResidue
BASP1131
BASP1135
BARG1137
BASP1140
BSER1141
BLEU1143
BASP1145
BTYR1211
BARG1214
BPHE1215
DARG1189

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 1
ChainResidue
CZN2
CCYS1031
CCYS1044
CCYS1074
CCYS1078

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 2
ChainResidue
CZN1
CZN3
CCYS1037
CCYS1074
CCYS1080
CCYS1084

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 3
ChainResidue
CZN2
CCYS1031
CCYS1033
CCYS1037
CCYS1042

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 4
ChainResidue
CCYS1172
CCYS1225
CCYS1227
CCYS1232

site_idBC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SAH C 103
ChainResidue
CMET1105
CTRP1107
CSER1141
CTYR1142
CARG1166
CPHE1167
CASN1169
CHIS1170
CTYR1211
CCYS1225
CARG1226

site_idBC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE E67 C 1236
ChainResidue
CASP1140
CSER1141
CLEU1143
CASP1145
CTYR1211
CARG1214
CPHE1215
CLYS1219
AARG1189
CASP1131
CASP1135
CARG1137

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN D 5
ChainResidue
DZN6
DZN7
DHOH295
DCYS1031
DCYS1044
DCYS1074
DCYS1078

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN D 6
ChainResidue
DZN5
DHOH295
DCYS1037
DCYS1074
DCYS1080
DCYS1084

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN D 7
ChainResidue
DZN5
DHOH295
DCYS1031
DCYS1033
DCYS1037
DCYS1042

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 8
ChainResidue
DCYS1172
DCYS1225
DCYS1227
DCYS1232

site_idCC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAH D 104
ChainResidue
DMET1105
DGLY1106
DTRP1107
DSER1141
DTYR1142
DARG1166
DASN1169
DHIS1170
DTYR1211
DPHE1215
DPHE1223
DSER1224
DCYS1225
DARG1226

site_idCC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE E67 D 4
ChainResidue
DASP1131
DASP1135
DVAL1136
DARG1137
DASP1140
DSER1141
DLEU1143
DASP1145
DTYR1211
DARG1214
DPHE1215
DLYS1219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues52
DetailsBINDING:
ChainResidueDetails
AGLU1062
AALA1203
BGLU1062
BASN1064
BPRO1068
BGLU1073
BASN1075
BMET1105
BVAL1109
BSER1111
BILE1115
BVAL1136
BGLU1173
BLEU1200
BALA1203
CGLU1062
CASN1064
CPRO1068
CGLU1073
CASN1075
CMET1105
CVAL1109
CSER1111
CILE1115
CVAL1136
CGLU1173
CLEU1200
CALA1203
DGLU1062
DASN1064
DPRO1068
DGLU1073
DASN1075
DMET1105
DVAL1109
DSER1111
DILE1115
DVAL1136
DGLU1173
DLEU1200
DALA1203
AASN1064
APRO1068
AGLU1073
AASN1075
AMET1105
AVAL1109
ASER1111
AILE1115
AVAL1136
AGLU1173
ALEU1200

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Histone H3K9me binding => ECO:0000269|PubMed:18264113, ECO:0000269|PubMed:20084102
ChainResidueDetails
ACYS1155
BCYS1155
CCYS1155
DCYS1155

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO1004
ASER1048
BPRO1004
BSER1048
CPRO1004
CSER1048
DPRO1004
DSER1048

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PDB entries from 2024-06-12

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