6MBK
SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, First P212121 Crystal Form
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 601 |
Chain | Residue |
A | ARG74 |
A | CYS276 |
A | ASN277 |
A | HIS278 |
A | TYR312 |
A | SER324 |
A | PHE326 |
A | GOL609 |
A | HOH764 |
A | HOH782 |
A | HOH935 |
A | GLU102 |
A | HOH944 |
Y | HIS73 |
A | GLU103 |
A | PHE105 |
A | PRO179 |
A | THR252 |
A | ARG253 |
A | ASP274 |
A | MET275 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 602 |
Chain | Residue |
A | PRO42 |
A | GLU45 |
A | ILE202 |
A | HOH787 |
A | HOH840 |
A | HOH907 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | PRO42 |
A | GLY43 |
A | LEU399 |
A | GLY400 |
A | ASP401 |
A | SER402 |
A | ALA403 |
A | ARG406 |
A | HOH704 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue EDO A 604 |
Chain | Residue |
A | LYS64 |
A | GLY65 |
A | LEU66 |
A | HOH703 |
A | HOH707 |
A | HOH977 |
B | ASP71 |
B | LYS73 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 605 |
Chain | Residue |
A | ASN135 |
A | HOH731 |
A | HOH838 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 606 |
Chain | Residue |
A | PRO40 |
A | GLU45 |
A | GLU48 |
A | HIS203 |
A | SER207 |
A | LYS210 |
A | HOH717 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 607 |
Chain | Residue |
A | VAL458 |
A | LYS461 |
A | LYS465 |
A | HOH982 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue GOL A 608 |
Chain | Residue |
A | ASN317 |
A | PHE327 |
A | ASP334 |
A | PHE371 |
A | GLY469 |
A | GLU472 |
A | HOH763 |
A | HOH793 |
A | HOH900 |
A | HOH966 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue GOL A 609 |
Chain | Residue |
A | GLU103 |
A | PRO179 |
A | GLU181 |
A | TYR182 |
A | SAH601 |
A | HOH748 |
A | HOH842 |
A | HOH908 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 610 |
Chain | Residue |
A | ARG194 |
A | GLN197 |
A | LYS441 |
A | HOH752 |
A | HOH955 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 611 |
Chain | Residue |
A | PHE367 |
A | ALA368 |
A | HIS370 |
A | SER377 |
A | GLN379 |
A | HOH712 |
A | HOH718 |
site_id | AD3 |
Number of Residues | 23 |
Details | binding site for residue SAH B 1001 |
Chain | Residue |
B | HIS278 |
B | TYR312 |
B | SER324 |
B | PHE326 |
B | HOH1113 |
B | HOH1253 |
B | HOH1264 |
B | HOH1290 |
B | HOH1306 |
B | HOH1308 |
B | HOH1358 |
Z | HIS73 |
B | ARG74 |
B | GLU102 |
B | GLU103 |
B | PHE105 |
B | PRO179 |
B | THR252 |
B | ARG253 |
B | ASP274 |
B | MET275 |
B | CYS276 |
B | ASN277 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue EDO B 1002 |
Chain | Residue |
B | PRO42 |
B | GLU45 |
B | ILE202 |
B | PHE206 |
B | EDO1008 |
B | HOH1115 |
B | HOH1168 |
B | HOH1257 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 1003 |
Chain | Residue |
B | VAL297 |
B | HOH1341 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue EDO B 1004 |
Chain | Residue |
B | PHE70 |
B | ARG164 |
B | ILE175 |
B | GLN176 |
B | LEU178 |
B | PRO179 |
B | SER180 |
B | HOH1231 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue EDO B 1005 |
Chain | Residue |
B | ASN484 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO B 1006 |
Chain | Residue |
B | ASP76 |
B | TYR77 |
B | ASP80 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue EDO B 1007 |
Chain | Residue |
B | ASP334 |
B | PHE371 |
B | GLY469 |
B | GLU472 |
B | ILE473 |
B | HOH1224 |
site_id | AE1 |
Number of Residues | 10 |
Details | binding site for residue EDO B 1008 |
Chain | Residue |
B | PRO42 |
B | GLY43 |
B | LEU399 |
B | GLY400 |
B | ASP401 |
B | SER402 |
B | ALA403 |
B | ARG406 |
B | EDO1002 |
B | HOH1106 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue EDO B 1009 |
Chain | Residue |
B | GLN200 |
B | LYS337 |
B | LYS339 |
B | LEU436 |
B | HOH1198 |
B | HOH1222 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue GOL B 1010 |
Chain | Residue |
B | HIS203 |
B | ASP401 |
B | HOH1144 |
site_id | AE4 |
Number of Residues | 9 |
Details | binding site for residue GOL B 1011 |
Chain | Residue |
B | HIS370 |
B | PHE371 |
B | THR372 |
B | GLU373 |
B | PRO375 |
B | LYS476 |
B | ALA477 |
B | SER480 |
B | HOH1136 |
site_id | AE5 |
Number of Residues | 9 |
Details | binding site for residue SO4 B 1012 |
Chain | Residue |
B | PHE367 |
B | ALA368 |
B | HIS370 |
B | SER377 |
B | GLN379 |
B | HOH1101 |
B | HOH1110 |
B | HOH1128 |
B | HOH1133 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 1013 |
Chain | Residue |
B | ARG194 |
B | LYS441 |
B | HOH1163 |
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 |