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 | 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 | 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 | 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 | 2 |
| Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"30526847","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30785395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31388018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32503840","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 440 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30785395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31388018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31911441","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31993215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32503840","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human SET domain-containing protein 3.","authors":["Zeng H.","Dong A.","Walker J.R.","Loppnau P.","Bountra C.","Weigelt J.","Arrowsmith C.H.","Edwards A.M.","Min J.","Wu H."]}},{"source":"PDB","id":"3SMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ICT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ICV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V62","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WK2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
