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5V9J

Crystal structure of catalytic domain of GLP with MS0105

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 Residues17
Detailsbinding site for residue SAM A 1301
ChainResidue
AMET1136
ATYR1242
APHE1246
APHE1254
ACYS1256
AARG1257
AHOH1511
AHOH1553
AHOH1574
AGLY1137
ATRP1138
ASER1172
ATYR1173
AARG1197
APHE1198
AASN1200
AHIS1201

site_idAC2
Number of Residues13
Detailsbinding site for residue 90P A 1302
ChainResidue
AASP1162
AALA1165
AASP1166
AARG1168
AASP1171
ALEU1174
AASP1176
AVAL1184
ACYS1186
AARG1245
APHE1246
AILE1249
ALYS1250

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1303
ChainResidue
ACYS1062
ACYS1075
ACYS1105
ACYS1109

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1304
ChainResidue
ACYS1068
ACYS1105
ACYS1111
ACYS1115

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 1305
ChainResidue
ACYS1062
ACYS1064
ACYS1068
ACYS1073

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN A 1306
ChainResidue
ACYS1203
ACYS1256
ACYS1258
ACYS1263

site_idAC7
Number of Residues5
Detailsbinding site for residue CL A 1307
ChainResidue
AVAL1119
AASN1122
AARG1125
BLYS1262
BHOH1579

site_idAC8
Number of Residues2
Detailsbinding site for residue CL A 1308
ChainResidue
AARG1054
AHOH1601

site_idAC9
Number of Residues18
Detailsbinding site for residue SAM B 1301
ChainResidue
BMET1136
BTRP1138
BSER1172
BTYR1173
BARG1197
BPHE1198
BASN1200
BHIS1201
BTYR1242
BPHE1246
BPHE1254
BCYS1256
BARG1257
BHOH1460
BHOH1500
BHOH1504
BHOH1557
BHOH1561

site_idAD1
Number of Residues14
Detailsbinding site for residue 90P B 1302
ChainResidue
BGLN1144
BALA1165
BASP1166
BARG1168
BASP1171
BLEU1174
BASP1176
BVAL1184
BCYS1186
BARG1245
BPHE1246
BILE1249
BLYS1250
BHOH1558

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 1303
ChainResidue
BCYS1062
BCYS1075
BCYS1105
BCYS1109

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN B 1304
ChainResidue
BCYS1068
BCYS1105
BCYS1111
BCYS1115

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN B 1305
ChainResidue
BCYS1062
BCYS1064
BCYS1068
BCYS1073

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN B 1306
ChainResidue
BCYS1258
BCYS1263
BCYS1203
BCYS1256

site_idAD6
Number of Residues2
Detailsbinding site for residue CL B 1307
ChainResidue
BARG1054
BHOH1596

site_idAD7
Number of Residues5
Detailsbinding site for residue DMS B 1308
ChainResidue
ALEU1078
BCYS1064
BILE1065
BASP1066
BSER1070

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 Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1004
ASER1048
BSER1004
BSER1048

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PDB entries from 2024-07-24

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