8EII
Cryo-EM structure of human DNMT3B homo-tetramer (form II)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009008 | molecular_function | DNA-methyltransferase activity |
| A | 0010468 | biological_process | regulation of gene expression |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009008 | molecular_function | DNA-methyltransferase activity |
| B | 0010468 | biological_process | regulation of gene expression |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0009008 | molecular_function | DNA-methyltransferase activity |
| C | 0010468 | biological_process | regulation of gene expression |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0009008 | molecular_function | DNA-methyltransferase activity |
| D | 0010468 | biological_process | regulation of gene expression |
Functional Information from PROSITE/UniProt
| site_id | PS00094 |
| Number of Residues | 13 |
| Details | C5_MTASE_1 C-5 cytosine-specific DNA methylases active site. DlVigGsPCnDLS |
| Chain | Residue | Details |
| A | ASP643-SER655 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 396 |
| Details | Domain: {"description":"ADD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00865","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 90 |
| Details | Zinc finger: {"description":"GATA-type; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00865","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 168 |
| Details | Zinc finger: {"description":"PHD-type; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00865","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 276 |
| Details | Region: {"description":"Interaction with the PRC2/EED-EZH2 complex","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01016","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10018","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y6K1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Citrulline","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
