6OX4
A SETD3 Mutant (N255A) in Complex with an Actin Peptide
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 | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0016740 | molecular_function | transferase 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 | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| B | 0016740 | molecular_function | transferase 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 | 3 |
| Details | binding site for residue EDO Y 101 |
| Chain | Residue |
| A | ASN153 |
| Y | THR77 |
| Y | ASN78 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 601 |
| Chain | Residue |
| A | MET275 |
| A | CYS276 |
| A | ASN277 |
| A | HIS278 |
| A | TYR312 |
| A | SER324 |
| A | PHE326 |
| A | PHE328 |
| A | GOL619 |
| A | HOH751 |
| A | HOH803 |
| A | HOH804 |
| A | HOH815 |
| A | ARG74 |
| A | GLU103 |
| A | PHE105 |
| A | PRO179 |
| A | ARG253 |
| A | ASP274 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | EDO610 |
| A | HOH746 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | SER316 |
| A | ASN317 |
| A | ALA318 |
| A | ASP334 |
| A | ARG335 |
| A | VAL336 |
| A | LEU466 |
| A | GLU470 |
| A | EDO606 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | ASP204 |
| A | ALA318 |
| A | GLU319 |
| A | EDO606 |
| A | HOH704 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | ALA378 |
| A | ILE407 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | SER316 |
| A | ALA318 |
| A | GLU319 |
| A | ARG335 |
| A | EDO603 |
| A | EDO604 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 607 |
| Chain | Residue |
| A | LEU451 |
| A | HIS454 |
| A | LEU456 |
| A | LYS461 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | GLN256 |
| A | ILE257 |
| A | PRO258 |
| A | VAL265 |
| Y | TYR69 |
| Y | PRO70 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 609 |
| Chain | Residue |
| A | ASP334 |
| A | GLU472 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 610 |
| Chain | Residue |
| A | LYS448 |
| A | GLU472 |
| A | EDO602 |
| A | HOH746 |
| A | HOH862 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 611 |
| Chain | Residue |
| A | ARG60 |
| A | LYS61 |
| A | GLN63 |
| A | HOH716 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 612 |
| Chain | Residue |
| A | ILE24 |
| A | GLN63 |
| A | TYR220 |
| A | SER237 |
| A | PHE238 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 613 |
| Chain | Residue |
| A | SER364 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 614 |
| Chain | Residue |
| A | ARG53 |
| A | GLU190 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 615 |
| Chain | Residue |
| A | PHE327 |
| A | VAL458 |
| A | LYS465 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 616 |
| Chain | Residue |
| A | LEU399 |
| A | GLY400 |
| A | ASP401 |
| A | SER402 |
| A | ALA403 |
| A | ARG406 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 617 |
| Chain | Residue |
| A | ASP401 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 618 |
| Chain | Residue |
| A | LYS125 |
| A | TRP171 |
| A | HOH750 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 619 |
| Chain | Residue |
| A | GLU103 |
| A | GLU181 |
| A | TYR182 |
| A | SAH601 |
| A | HOH783 |
| A | HOH823 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 620 |
| Chain | Residue |
| A | ILE338 |
| A | LYS339 |
| A | ARG432 |
| A | HOH725 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 621 |
| Chain | Residue |
| A | ALA368 |
| A | SER377 |
| A | HOH764 |
| A | PHE367 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 622 |
| Chain | Residue |
| A | GLN197 |
| A | SER198 |
| A | PHE206 |
| A | HOH822 |
| A | HOH844 |
| site_id | AE6 |
| Number of Residues | 19 |
| Details | binding site for residue SAH B 601 |
| Chain | Residue |
| B | ARG74 |
| B | GLU102 |
| B | GLU103 |
| B | PHE105 |
| B | PRO179 |
| B | ARG253 |
| B | ASP274 |
| B | MET275 |
| B | CYS276 |
| B | ASN277 |
| B | HIS278 |
| B | TYR312 |
| B | SER324 |
| B | PHE326 |
| B | HOH779 |
| B | HOH799 |
| B | HOH802 |
| B | HOH815 |
| B | HOH818 |
| site_id | AE7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| B | ILE407 |
| site_id | AE8 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 603 |
| Chain | Residue |
| B | MET462 |
| site_id | AE9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 604 |
| Chain | Residue |
| B | ARG60 |
| B | LYS61 |
| B | GLN63 |
| site_id | AF1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 605 |
| Chain | Residue |
| A | LYS101 |
| B | GLU102 |
| B | EDO616 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 606 |
| Chain | Residue |
| B | LEU340 |
| B | GLY341 |
| B | PHE387 |
| B | ARG432 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 607 |
| Chain | Residue |
| A | SER86 |
| B | MET82 |
| B | LYS83 |
| B | SER86 |
| B | HOH722 |
| B | HOH816 |
| site_id | AF4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 608 |
| Chain | Residue |
| B | ALA318 |
| B | ASP334 |
| B | ARG335 |
| B | LEU466 |
| B | GLY469 |
| B | GLU470 |
| site_id | AF5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 609 |
| Chain | Residue |
| B | HIS333 |
| site_id | AF6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 610 |
| Chain | Residue |
| B | GLN63 |
| B | TYR220 |
| B | PHE238 |
| site_id | AF7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 611 |
| Chain | Residue |
| A | ASP71 |
| B | LYS64 |
| B | GLY65 |
| B | LEU66 |
| B | THR69 |
| site_id | AF8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 612 |
| Chain | Residue |
| B | HIS397 |
| B | ARG406 |
| B | THR409 |
| B | PHE415 |
| site_id | AF9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 613 |
| Chain | Residue |
| A | LYS73 |
| B | ARG60 |
| B | TYR187 |
| B | ARG244 |
| B | HOH711 |
| B | HOH739 |
| B | HOH757 |
| site_id | AG1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 614 |
| Chain | Residue |
| B | TRP121 |
| B | ARG293 |
| site_id | AG2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 615 |
| Chain | Residue |
| B | SER364 |
| site_id | AG3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 616 |
| Chain | Residue |
| B | ASP183 |
| B | ARG459 |
| B | EDO605 |
| B | HOH809 |
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 |
