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6OX1

SETD3 in Complex with an Actin Peptide with Target Histidine Partially Methylated

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003713molecular_functiontranscription coactivator activity
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0018021biological_processpeptidyl-histidine methylation
A0018023biological_processpeptidyl-lysine trimethylation
A0018064molecular_functionprotein-L-histidine N-tele-methyltransferase activity
A0030047biological_processactin modification
A0032259biological_processmethylation
A0042800molecular_functionhistone H3K4 methyltransferase activity
A0045893biological_processpositive regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046975molecular_functionhistone H3K36 methyltransferase activity
A0051149biological_processpositive regulation of muscle cell differentiation
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0070472biological_processregulation of uterine smooth muscle contraction
B0000785cellular_componentchromatin
B0003713molecular_functiontranscription coactivator activity
B0003779molecular_functionactin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006338biological_processchromatin remodeling
B0008168molecular_functionmethyltransferase activity
B0008170molecular_functionN-methyltransferase activity
B0008276molecular_functionprotein methyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0018021biological_processpeptidyl-histidine methylation
B0018023biological_processpeptidyl-lysine trimethylation
B0018064molecular_functionprotein-L-histidine N-tele-methyltransferase activity
B0030047biological_processactin modification
B0032259biological_processmethylation
B0042800molecular_functionhistone H3K4 methyltransferase activity
B0045893biological_processpositive regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046975molecular_functionhistone H3K36 methyltransferase activity
B0051149biological_processpositive regulation of muscle cell differentiation
B0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
B0070472biological_processregulation of uterine smooth muscle contraction
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue SAH A 1001
ChainResidue
AARG74
AASN277
AHIS278
ATYR312
ASER324
APHE326
AHOH1219
AHOH1233
AHOH1238
AHOH1249
AHOH1261
AGLU102
AHOH1344
YHIC73
AGLU103
APHE105
APRO179
ATHR252
AARG253
AASP274
AMET275

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 1002
ChainResidue
ALYS448
AHOH1187
AHOH1227
AHOH1313

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 1003
ChainResidue
AASP204
AGLU319
AHIS323
AEDO1004
AHOH1150

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 1004
ChainResidue
AGLN200
AASP204
AALA318
ALYS337
AGLU470
AEDO1003
AEDO1016

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 1005
ChainResidue
AASP76
AASP80
BLYS61
BEDO1007

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 1006
ChainResidue
AILE24
AGLN63
ATYR220
ASER237
APHE238

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 1007
ChainResidue
AGLU96
AMET97
AHOH1162

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 1008
ChainResidue
AVAL458
ALYS461
ALYS465

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 1009
ChainResidue
ALEU340
AGLY341
AARG432
AHOH1120

site_idAD1
Number of Residues8
Detailsbinding site for residue EDO A 1010
ChainResidue
AASP334
APHE371
AGLY469
AGLU472
AILE473
AHOH1108
AHOH1136
AHOH1221

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO A 1011
ChainResidue
ALEU399
AGLY400
AASP401
ASER402
AALA403
AARG406
AHOH1267

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO A 1012
ChainResidue
AILE113
AASP301
AARG303
BLYS114

site_idAD4
Number of Residues2
Detailsbinding site for residue EDO A 1013
ChainResidue
AASN168
APHE170

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO A 1014
ChainResidue
AILE147
AARG214
AGLN215
YTRP79
YASP80

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO A 1015
ChainResidue
AMET82
ASER86
AHOH1225
AHOH1228
BSER86

site_idAD7
Number of Residues8
Detailsbinding site for residue EDO A 1016
ChainResidue
AASN317
AALA318
AASP334
AARG335
AVAL336
ALEU466
AGLU470
AEDO1004

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO A 1017
ChainResidue
AALA350
AGLU354

site_idAD9
Number of Residues21
Detailsbinding site for residue SAH B 1001
ChainResidue
BPHE105
BPRO179
BTHR252
BARG253
BASP274
BMET275
BCYS276
BASN277
BHIS278
BTYR312
BSER324
BPHE326
BHOH1208
BHOH1209
BHOH1260
BHOH1287
BHOH1323
BHOH1348
ZHIC73
BARG74
BGLU103

site_idAE1
Number of Residues4
Detailsbinding site for residue EDO B 1002
ChainResidue
BALA359
BALA378
BGLN379
BILE407

site_idAE2
Number of Residues4
Detailsbinding site for residue EDO B 1003
ChainResidue
BLEU340
BGLY341
BARG432
BHOH1241

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO B 1004
ChainResidue
BPRO40
BGLU48
BSER207
BLYS210

site_idAE4
Number of Residues4
Detailsbinding site for residue EDO B 1005
ChainResidue
BASP80
BLYS83
BTRP84
BGLU87

site_idAE5
Number of Residues2
Detailsbinding site for residue EDO B 1006
ChainResidue
BGLU354
BALA357

site_idAE6
Number of Residues6
Detailsbinding site for residue EDO B 1007
ChainResidue
AGLY72
AASP76
AEDO1005
BARG60
BLYS61
BGLN63

site_idAE7
Number of Residues5
Detailsbinding site for residue EDO B 1008
ChainResidue
BPRO179
BSER180
BGLU181
BHOH1189
BHOH1247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215, ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12, ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT, ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT, ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK, ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0, ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2, ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4, ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62, ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1, ECO:0007744|PDB:6WK2
ChainResidueDetails
AARG74
BSER324
AGLU103
AARG253
AASP274
ASER324
BARG74
BGLU103
BARG253
BASP274

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER512
BSER512

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PDB entries from 2024-06-26

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