6OX1
SETD3 in Complex with an Actin Peptide with Target Histidine Partially Methylated
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000785 | cellular_component | chromatin |
A | 0003713 | molecular_function | transcription coactivator activity |
A | 0003779 | molecular_function | actin binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0006338 | biological_process | chromatin remodeling |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008170 | molecular_function | N-methyltransferase activity |
A | 0008276 | molecular_function | protein methyltransferase activity |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
A | 0018021 | biological_process | peptidyl-histidine methylation |
A | 0018023 | biological_process | peptidyl-lysine trimethylation |
A | 0018064 | molecular_function | protein-L-histidine N-tele-methyltransferase activity |
A | 0030047 | biological_process | actin modification |
A | 0032259 | biological_process | methylation |
A | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
A | 0046975 | molecular_function | histone H3K36 methyltransferase activity |
A | 0051149 | biological_process | positive regulation of muscle cell differentiation |
A | 0061629 | molecular_function | RNA polymerase II-specific DNA-binding transcription factor binding |
A | 0070472 | biological_process | regulation of uterine smooth muscle contraction |
B | 0000785 | cellular_component | chromatin |
B | 0003713 | molecular_function | transcription coactivator activity |
B | 0003779 | molecular_function | actin binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0006338 | biological_process | chromatin remodeling |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008170 | molecular_function | N-methyltransferase activity |
B | 0008276 | molecular_function | protein methyltransferase activity |
B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
B | 0018021 | biological_process | peptidyl-histidine methylation |
B | 0018023 | biological_process | peptidyl-lysine trimethylation |
B | 0018064 | molecular_function | protein-L-histidine N-tele-methyltransferase activity |
B | 0030047 | biological_process | actin modification |
B | 0032259 | biological_process | methylation |
B | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
B | 0046975 | molecular_function | histone H3K36 methyltransferase activity |
B | 0051149 | biological_process | positive regulation of muscle cell differentiation |
B | 0061629 | molecular_function | RNA polymerase II-specific DNA-binding transcription factor binding |
B | 0070472 | biological_process | regulation of uterine smooth muscle contraction |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue SAH A 1001 |
Chain | Residue |
A | ARG74 |
A | ASN277 |
A | HIS278 |
A | TYR312 |
A | SER324 |
A | PHE326 |
A | HOH1219 |
A | HOH1233 |
A | HOH1238 |
A | HOH1249 |
A | HOH1261 |
A | GLU102 |
A | HOH1344 |
Y | HIC73 |
A | GLU103 |
A | PHE105 |
A | PRO179 |
A | THR252 |
A | ARG253 |
A | ASP274 |
A | MET275 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue GOL A 1002 |
Chain | Residue |
A | LYS448 |
A | HOH1187 |
A | HOH1227 |
A | HOH1313 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 1003 |
Chain | Residue |
A | ASP204 |
A | GLU319 |
A | HIS323 |
A | EDO1004 |
A | HOH1150 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 1004 |
Chain | Residue |
A | GLN200 |
A | ASP204 |
A | ALA318 |
A | LYS337 |
A | GLU470 |
A | EDO1003 |
A | EDO1016 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 1005 |
Chain | Residue |
A | ASP76 |
A | ASP80 |
B | LYS61 |
B | EDO1007 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 1006 |
Chain | Residue |
A | ILE24 |
A | GLN63 |
A | TYR220 |
A | SER237 |
A | PHE238 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 1007 |
Chain | Residue |
A | GLU96 |
A | MET97 |
A | HOH1162 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO A 1008 |
Chain | Residue |
A | VAL458 |
A | LYS461 |
A | LYS465 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 1009 |
Chain | Residue |
A | LEU340 |
A | GLY341 |
A | ARG432 |
A | HOH1120 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue EDO A 1010 |
Chain | Residue |
A | ASP334 |
A | PHE371 |
A | GLY469 |
A | GLU472 |
A | ILE473 |
A | HOH1108 |
A | HOH1136 |
A | HOH1221 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 1011 |
Chain | Residue |
A | LEU399 |
A | GLY400 |
A | ASP401 |
A | SER402 |
A | ALA403 |
A | ARG406 |
A | HOH1267 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 1012 |
Chain | Residue |
A | ILE113 |
A | ASP301 |
A | ARG303 |
B | LYS114 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue EDO A 1013 |
Chain | Residue |
A | ASN168 |
A | PHE170 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 1014 |
Chain | Residue |
A | ILE147 |
A | ARG214 |
A | GLN215 |
Y | TRP79 |
Y | ASP80 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 1015 |
Chain | Residue |
A | MET82 |
A | SER86 |
A | HOH1225 |
A | HOH1228 |
B | SER86 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue EDO A 1016 |
Chain | Residue |
A | ASN317 |
A | ALA318 |
A | ASP334 |
A | ARG335 |
A | VAL336 |
A | LEU466 |
A | GLU470 |
A | EDO1004 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue EDO A 1017 |
Chain | Residue |
A | ALA350 |
A | GLU354 |
site_id | AD9 |
Number of Residues | 21 |
Details | binding site for residue SAH B 1001 |
Chain | Residue |
B | PHE105 |
B | PRO179 |
B | THR252 |
B | ARG253 |
B | ASP274 |
B | MET275 |
B | CYS276 |
B | ASN277 |
B | HIS278 |
B | TYR312 |
B | SER324 |
B | PHE326 |
B | HOH1208 |
B | HOH1209 |
B | HOH1260 |
B | HOH1287 |
B | HOH1323 |
B | HOH1348 |
Z | HIC73 |
B | ARG74 |
B | GLU103 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue EDO B 1002 |
Chain | Residue |
B | ALA359 |
B | ALA378 |
B | GLN379 |
B | ILE407 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 1003 |
Chain | Residue |
B | LEU340 |
B | GLY341 |
B | ARG432 |
B | HOH1241 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue EDO B 1004 |
Chain | Residue |
B | PRO40 |
B | GLU48 |
B | SER207 |
B | LYS210 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 1005 |
Chain | Residue |
B | ASP80 |
B | LYS83 |
B | TRP84 |
B | GLU87 |
site_id | AE5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 1006 |
Chain | Residue |
B | GLU354 |
B | ALA357 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 1007 |
Chain | Residue |
A | GLY72 |
A | ASP76 |
A | EDO1005 |
B | ARG60 |
B | LYS61 |
B | GLN63 |
site_id | AE7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 1008 |
Chain | Residue |
B | PRO179 |
B | SER180 |
B | GLU181 |
B | HOH1189 |
B | HOH1247 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ARG74 | |
B | SER324 | |
A | GLU103 | |
A | ARG253 | |
A | ASP274 | |
A | SER324 | |
B | ARG74 | |
B | GLU103 | |
B | ARG253 | |
B | ASP274 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER512 | |
B | SER512 |