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5TUZ

Structure of human GLP SET-domain (EHMT1) in complex with inhibitor MS0124

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
B0002039molecular_functionp53 binding
B0005634cellular_componentnucleus
B0008270molecular_functionzinc ion binding
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0042054molecular_functionhistone methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue SAM A 3001
ChainResidue
AMET1136
APHE1246
ACYS1256
AARG1257
AHOH3110
AHOH3191
AHOH3201
AHOH3209
AGLY1137
ATRP1138
ASER1172
ATYR1173
AARG1197
AASN1200
AHIS1201
ATYR1242

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 3002
ChainResidue
ACYS1062
ACYS1075
ACYS1105
ACYS1109

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 3003
ChainResidue
ACYS1068
ACYS1105
ACYS1111
ACYS1115

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 3004
ChainResidue
ACYS1062
ACYS1064
ACYS1068
ACYS1073

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 3005
ChainResidue
ACYS1203
ACYS1256
ACYS1258
ACYS1263

site_idAC6
Number of Residues11
Detailsbinding site for residue 7L6 A 3006
ChainResidue
AASP1162
AALA1165
AASP1166
AARG1168
AASP1171
ALEU1174
AASP1176
ACYS1186
AARG1245
APHE1246
AILE1249

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 3007
ChainResidue
ACYS1064
AILE1065
AASP1066
AASN1072
BLEU1078
BPHE1103

site_idAC8
Number of Residues16
Detailsbinding site for residue SAM B 3001
ChainResidue
BMET1136
BGLY1137
BTRP1138
BSER1172
BTYR1173
BARG1197
BASN1200
BHIS1201
BTYR1242
BPHE1246
BCYS1256
BARG1257
BHOH3164
BHOH3167
BHOH3172
BHOH3179

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 3002
ChainResidue
BCYS1062
BCYS1075
BCYS1105
BCYS1109

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 3003
ChainResidue
BCYS1068
BCYS1105
BCYS1111
BCYS1115

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 3004
ChainResidue
BCYS1062
BCYS1064
BCYS1068
BCYS1073

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN B 3005
ChainResidue
BCYS1203
BCYS1256
BCYS1258
BCYS1263

site_idAD4
Number of Residues12
Detailsbinding site for residue 7L6 B 3006
ChainResidue
BASP1162
BALA1165
BASP1166
BARG1168
BASP1171
BLEU1174
BASP1176
BCYS1186
BARG1245
BPHE1246
BILE1249
BLYS1250

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO B 3007
ChainResidue
AARG1054
BARG1054

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsBINDING:
ChainResidueDetails
ACYS1062
AMET1136
ATYR1173
AASN1200
ACYS1203
ACYS1256
AARG1257
ACYS1258
ACYS1263
BCYS1062
BCYS1064
ACYS1064
BCYS1068
BCYS1073
BCYS1075
BCYS1105
BCYS1109
BCYS1111
BCYS1115
BMET1136
BTYR1173
BASN1200
ACYS1068
BCYS1203
BCYS1256
BARG1257
BCYS1258
BCYS1263
ACYS1073
ACYS1075
ACYS1105
ACYS1109
ACYS1111
ACYS1115

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Histone H3K9me binding => ECO:0000269|PubMed:18264113, ECO:0000269|PubMed:20084102
ChainResidueDetails
ATYR1155
BTYR1155

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1048
BSER1048

219515

PDB entries from 2024-05-08

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