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3MO0

Human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E11

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 Residues11
DetailsBINDING SITE FOR RESIDUE SAH A 101
ChainResidue
AMET1105
APHE1223
AARG1226
AGLY1106
ATRP1107
ASER1141
ATYR1142
AARG1166
AASN1169
AHIS1170
ATYR1211

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE E11 A 2001
ChainResidue
AASN1083
AASP1131
AALA1134
AASP1135
AGLU1138
AASP1140
ALEU1143
AASP1145
AARG1214
APHE1215
AILE1218

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1236
ChainResidue
AZN3
ACYS1031
ACYS1044
ACYS1074
ACYS1078

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AZN3
ACYS1037
ACYS1074
ACYS1080
ACYS1084

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
AZN2
ACYS1031
ACYS1033
ACYS1037
ACYS1042
AZN1236

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 4
ChainResidue
ACYS1172
ACYS1225
ACYS1227
ACYS1232

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 10
ChainResidue
AHIS1027
AHIS1076
AHIS1185
BCYS1014

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE E11 A 2002
ChainResidue
AASP1131
AALA1134
AARG1137
AGLU1138
AASP1140
ALEU1143
AASP1145
AARG1214
APHE1215
AILE1218

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1
ChainResidue
ASER1132
AASP1135
AVAL1136
BGLY986
BGLU988
BPRO991

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 2
ChainResidue
BILE983
BARG985
BTYR1007
BTYR1009

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SAH B 102
ChainResidue
BMET1105
BGLY1106
BTRP1107
BSER1141
BTYR1142
BARG1166
BASN1169
BHIS1170
BTYR1211
BPHE1223
BARG1226
BCYS1227

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE E11 B 2003
ChainResidue
BALA1134
BASP1135
BARG1137
BASP1140
BLEU1143
BASP1145
BPHE1215
BILE1218

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 5
ChainResidue
BCYS1031
BCYS1044
BCYS1074
BCYS1078

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 6
ChainResidue
BCYS1037
BCYS1074
BCYS1080
BCYS1084

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 7
ChainResidue
BCYS1031
BCYS1033
BCYS1037
BCYS1042

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 8
ChainResidue
BCYS1225
BCYS1227
BCYS1232
BCYS1172

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 9
ChainResidue
ACYS1014
BHIS1027
BHIS1076
BHIS1185

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 2024-04-24

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