6OX0
SETD3 in Complex with an Actin Peptide with Sinefungin Replacing SAH as Cofactor
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 | 19 |
| Details | binding site for residue SFG A 1001 |
| Chain | Residue |
| A | ARG74 |
| A | ASN277 |
| A | HIS278 |
| A | TYR312 |
| A | SER324 |
| A | PHE326 |
| A | HOH1224 |
| A | HOH1242 |
| A | HOH1285 |
| A | HOH1293 |
| Y | HIS73 |
| A | GLU102 |
| A | GLU103 |
| A | PHE105 |
| A | PRO179 |
| A | ARG253 |
| A | ASP274 |
| A | MET275 |
| A | CYS276 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 1002 |
| Chain | Residue |
| A | LYS448 |
| A | LEU451 |
| A | HOH1172 |
| A | HOH1276 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 1003 |
| Chain | Residue |
| A | ASP204 |
| A | HIS323 |
| A | EDO1004 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 1004 |
| Chain | Residue |
| A | GLN200 |
| A | ALA201 |
| A | ASP204 |
| A | ALA318 |
| A | LYS337 |
| A | GLU470 |
| A | EDO1003 |
| A | EDO1006 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 1005 |
| Chain | Residue |
| A | ILE24 |
| A | GLN63 |
| A | TYR220 |
| A | SER237 |
| A | PHE238 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 1006 |
| Chain | Residue |
| A | ASN317 |
| A | ALA318 |
| A | ASP334 |
| A | ARG335 |
| A | VAL336 |
| A | LEU466 |
| A | GLU470 |
| A | EDO1004 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 1007 |
| Chain | Residue |
| A | LEU340 |
| A | GLY341 |
| A | ARG432 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 1008 |
| Chain | Residue |
| A | GLU96 |
| A | MET97 |
| A | HOH1157 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1009 |
| Chain | Residue |
| A | PHE327 |
| A | VAL458 |
| A | LYS461 |
| A | LYS465 |
| A | HOH1193 |
| A | HOH1209 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1010 |
| Chain | Residue |
| A | GLN256 |
| A | ILE257 |
| A | PRO258 |
| A | VAL265 |
| Y | TYR69 |
| Y | PRO70 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 1011 |
| Chain | Residue |
| A | SER198 |
| A | HIS203 |
| A | PHE206 |
| A | HOH1194 |
| A | HOH1257 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1012 |
| Chain | Residue |
| A | LYS101 |
| A | GLU102 |
| A | VAL458 |
| A | HOH1193 |
| A | HOH1416 |
| B | LYS101 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 1013 |
| Chain | Residue |
| A | PHE367 |
| A | ALA368 |
| A | SER377 |
| A | HOH1120 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 1014 |
| Chain | Residue |
| A | ASP329 |
| A | ASN330 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 1015 |
| Chain | Residue |
| A | TRP121 |
| A | ARG293 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 1016 |
| Chain | Residue |
| A | HOH1150 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 1017 |
| Chain | Residue |
| A | ASP334 |
| A | PHE371 |
| A | GLY469 |
| A | GLU472 |
| A | ILE473 |
| A | HOH1104 |
| A | HOH1116 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 1018 |
| Chain | Residue |
| A | GLN200 |
| A | LYS337 |
| A | ILE338 |
| A | LYS339 |
| A | LEU436 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1019 |
| Chain | Residue |
| A | ASP401 |
| A | SER402 |
| A | ALA403 |
| A | ARG406 |
| A | LEU399 |
| A | GLY400 |
| site_id | AE2 |
| Number of Residues | 22 |
| Details | binding site for residue SFG B 1001 |
| Chain | Residue |
| B | ARG74 |
| B | GLU102 |
| B | GLU103 |
| 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 | HOH1196 |
| B | HOH1212 |
| B | HOH1266 |
| B | HOH1294 |
| B | HOH1304 |
| B | HOH1311 |
| Z | HIS73 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 1002 |
| Chain | Residue |
| B | ALA359 |
| B | ILE407 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1003 |
| Chain | Residue |
| B | TYR182 |
| B | ASP183 |
| B | HOH1222 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1004 |
| Chain | Residue |
| B | LEU340 |
| B | GLY341 |
| B | PHE387 |
| B | ARG432 |
| B | HOH1109 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1005 |
| Chain | Residue |
| B | HIS333 |
| B | ARG335 |
| B | HIS370 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 1006 |
| Chain | Residue |
| B | ASP191 |
| B | ASP291 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 1007 |
| Chain | Residue |
| B | LEU282 |
| B | THR284 |
| B | THR285 |
| B | ILE310 |
| B | PHE311 |
| Z | HOH103 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 1008 |
| Chain | Residue |
| B | THR314 |
| B | ARG315 |
| B | GLU319 |
| B | ARG335 |
| Z | VAL76 |
| Z | HOH105 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1009 |
| Chain | Residue |
| B | PRO40 |
| B | GLU48 |
| B | SER207 |
| B | LYS210 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1010 |
| Chain | Residue |
| B | ASP329 |
| B | VAL458 |
| B | LYS461 |
| B | MET462 |
| B | LYS465 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 1011 |
| Chain | Residue |
| A | GLY72 |
| A | ASP76 |
| B | ARG60 |
| B | LYS61 |
| B | GLN63 |
| B | HOH1182 |
| site_id | AF4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1012 |
| Chain | Residue |
| B | ASP334 |
| B | GLU472 |
| B | HOH1219 |
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 |
