6OX3
SETD3 in Complex with an Actin Peptide with His73 Replaced with Lysine
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 | 6 |
Details | binding site for residue GOL Y 101 |
Chain | Residue |
A | ASN153 |
Y | THR77 |
Y | ASN78 |
Y | LYS84 |
Y | HOH204 |
Y | HOH209 |
site_id | AC2 |
Number of Residues | 21 |
Details | binding site for residue SAH A 601 |
Chain | Residue |
A | PHE105 |
A | PRO179 |
A | THR252 |
A | ARG253 |
A | ASP274 |
A | MET275 |
A | CYS276 |
A | ASN277 |
A | HIS278 |
A | TYR312 |
A | SER324 |
A | PHE326 |
A | GOL603 |
A | HOH749 |
A | HOH839 |
A | HOH849 |
A | HOH850 |
Y | LYS73 |
A | ARG74 |
A | GLU102 |
A | GLU103 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 602 |
Chain | Residue |
A | LYS125 |
A | PHE170 |
A | TRP171 |
A | HOH778 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 603 |
Chain | Residue |
A | GLU103 |
A | PRO179 |
A | GLU181 |
A | TYR182 |
A | SAH601 |
A | HOH788 |
A | HOH799 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 604 |
Chain | Residue |
A | ILE338 |
A | LYS339 |
A | ARG432 |
A | HOH768 |
A | HOH886 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue GOL A 605 |
Chain | Residue |
A | TYR287 |
A | ASN288 |
A | LEU289 |
A | GLU290 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue EDO A 606 |
Chain | Residue |
A | LYS448 |
A | EDO617 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue EDO A 607 |
Chain | Residue |
A | SER316 |
A | ASN317 |
A | ALA318 |
A | ASP334 |
A | ARG335 |
A | VAL336 |
A | LEU466 |
A | GLU470 |
A | EDO609 |
A | EDO612 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO A 608 |
Chain | Residue |
A | ASP204 |
A | ALA318 |
A | GLU319 |
A | ILE322 |
A | HIS323 |
A | EDO609 |
A | EDO612 |
A | HOH754 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue EDO A 609 |
Chain | Residue |
A | GLN200 |
A | ALA201 |
A | ASP204 |
A | ALA318 |
A | LYS337 |
A | GLU470 |
A | EDO607 |
A | EDO608 |
A | EDO612 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 610 |
Chain | Residue |
A | ALA382 |
A | ILE407 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 611 |
Chain | Residue |
A | ILE113 |
A | LYS114 |
A | ASP301 |
A | PHE302 |
A | ARG303 |
B | LYS114 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 612 |
Chain | Residue |
A | SER316 |
A | ALA318 |
A | ARG335 |
A | VAL336 |
A | EDO607 |
A | EDO608 |
A | EDO609 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 613 |
Chain | Residue |
A | LEU451 |
A | HIS454 |
A | ASP455 |
A | LEU456 |
A | LYS461 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 614 |
Chain | Residue |
B | HOH720 |
A | LYS101 |
B | GLU102 |
B | PGE614 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue EDO A 615 |
Chain | Residue |
A | GLN256 |
A | ILE257 |
A | PRO258 |
A | VAL265 |
Y | TYR69 |
Y | PRO70 |
Y | ILE71 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue EDO A 616 |
Chain | Residue |
A | ASP334 |
A | GLU472 |
A | ILE473 |
A | HOH718 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue EDO A 617 |
Chain | Residue |
A | GLU472 |
A | EDO606 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue EDO A 618 |
Chain | Residue |
A | THR69 |
A | PHE70 |
A | ASP71 |
B | LYS64 |
B | LEU66 |
B | THR69 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 619 |
Chain | Residue |
A | GLU48 |
A | SER207 |
A | LYS210 |
A | HOH831 |
A | HOH866 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 620 |
Chain | Residue |
A | ARG60 |
A | LYS61 |
A | GLN63 |
B | GLY72 |
B | ASP76 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 621 |
Chain | Residue |
A | GLN63 |
A | TYR220 |
A | SER237 |
A | PHE238 |
site_id | AE5 |
Number of Residues | 1 |
Details | binding site for residue EDO A 622 |
Chain | Residue |
A | SER364 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 623 |
Chain | Residue |
A | PHE327 |
A | VAL458 |
A | LYS461 |
A | MET462 |
A | LYS465 |
A | EDO627 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 624 |
Chain | Residue |
A | LEU399 |
A | GLY400 |
A | ASP401 |
A | SER402 |
A | ALA403 |
A | ARG406 |
site_id | AE8 |
Number of Residues | 8 |
Details | binding site for residue EDO A 625 |
Chain | Residue |
A | TYR220 |
A | ILE223 |
A | GLN224 |
A | LEU234 |
A | LYS235 |
A | SER237 |
A | HOH835 |
A | HOH864 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue EDO A 626 |
Chain | Residue |
A | LEU340 |
A | GLY341 |
A | PHE387 |
A | ARG432 |
A | HOH886 |
site_id | AF1 |
Number of Residues | 8 |
Details | binding site for residue EDO A 627 |
Chain | Residue |
A | ASP183 |
A | GLY325 |
A | PHE326 |
A | PHE327 |
A | VAL458 |
A | MET462 |
A | EDO623 |
A | HOH749 |
site_id | AF2 |
Number of Residues | 5 |
Details | binding site for residue ACT A 628 |
Chain | Residue |
A | PHE367 |
A | ALA368 |
A | SER377 |
A | GLN379 |
A | HOH780 |
site_id | AF3 |
Number of Residues | 22 |
Details | binding site for residue SAH B 601 |
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 | PGE614 |
B | HOH751 |
B | HOH816 |
B | HOH827 |
B | HOH834 |
B | HOH838 |
Z | LYS73 |
site_id | AF4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 602 |
Chain | Residue |
B | ILE283 |
B | GLY313 |
B | THR314 |
B | HOH716 |
Z | GLU72 |
site_id | AF5 |
Number of Residues | 3 |
Details | binding site for residue EDO B 603 |
Chain | Residue |
B | ALA359 |
B | ILE407 |
B | HOH754 |
site_id | AF6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 604 |
Chain | Residue |
A | ASP76 |
B | ARG60 |
B | LYS61 |
B | GLN63 |
site_id | AF7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 605 |
Chain | Residue |
B | ASP183 |
B | ARG459 |
B | EDO610 |
B | HOH769 |
site_id | AF8 |
Number of Residues | 4 |
Details | binding site for residue EDO B 606 |
Chain | Residue |
B | LEU340 |
B | GLY341 |
B | PHE387 |
B | ARG432 |
site_id | AF9 |
Number of Residues | 3 |
Details | binding site for residue EDO B 607 |
Chain | Residue |
B | LYS83 |
B | HOH708 |
B | HOH709 |
site_id | AG1 |
Number of Residues | 7 |
Details | binding site for residue EDO B 608 |
Chain | Residue |
B | ASN317 |
B | ALA318 |
B | ASP334 |
B | ARG335 |
B | LEU466 |
B | GLY469 |
B | GLU470 |
site_id | AG2 |
Number of Residues | 2 |
Details | binding site for residue EDO B 609 |
Chain | Residue |
B | HIS333 |
B | ARG335 |
site_id | AG3 |
Number of Residues | 5 |
Details | binding site for residue EDO B 610 |
Chain | Residue |
B | PRO179 |
B | SER180 |
B | GLU181 |
B | EDO605 |
B | HOH895 |
site_id | AG4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 611 |
Chain | Residue |
B | GLN63 |
B | TYR220 |
B | SER237 |
B | PHE238 |
site_id | AG5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 612 |
Chain | Residue |
B | HIS397 |
B | ARG406 |
B | THR409 |
B | LEU410 |
B | PHE415 |
site_id | AG6 |
Number of Residues | 1 |
Details | binding site for residue EDO B 613 |
Chain | Residue |
B | ARG293 |
site_id | AG7 |
Number of Residues | 11 |
Details | binding site for residue PGE B 614 |
Chain | Residue |
A | EDO614 |
B | ASP183 |
B | GLY325 |
B | PHE326 |
B | PHE327 |
B | VAL458 |
B | LYS461 |
B | MET462 |
B | LYS465 |
B | SAH601 |
B | HOH769 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:32503840 |
Chain | Residue | Details |
Y | LYS73 | |
B | SER324 | |
Z | LYS73 | |
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: N6-methyllysine => ECO:0000269|PubMed:23673617 |
Chain | Residue | Details |
Y | LYS84 | |
Z | LYS84 |