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 | 120 |
| Details | ZN_FING: GATA-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00865 |
| Chain | Residue | Details |
| A | GLY434-GLU464 | |
| B | GLY434-GLU464 | |
| C | GLY434-GLU464 | |
| D | GLY434-GLU464 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 224 |
| Details | ZN_FING: PHD-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00865 |
| Chain | Residue | Details |
| A | GLN475-ARG531 | |
| B | GLN475-ARG531 | |
| C | GLN475-ARG531 | |
| D | GLN475-ARG531 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01016, ECO:0000255|PROSITE-ProRule:PRU10018 |
| Chain | Residue | Details |
| A | CYS651 | |
| B | CYS651 | |
| C | CYS651 | |
| D | CYS651 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Y6K1 |
| Chain | Residue | Details |
| A | ASP582 | |
| A | GLU605 | |
| A | ASP627 | |
| A | ARG832 | |
| B | ASP582 | |
| B | GLU605 | |
| B | ASP627 | |
| B | ARG832 | |
| C | ASP582 | |
| C | GLU605 | |
| C | ASP627 | |
| C | ARG832 | |
| D | ASP582 | |
| D | GLU605 | |
| D | ASP627 | |
| D | ARG832 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER209 | |
| B | SER209 | |
| C | SER209 | |
| D | SER209 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Citrulline => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG410 | |
| B | ARG410 | |
| C | ARG410 | |
| D | ARG410 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS617 | |
| B | LYS617 | |
| C | LYS617 | |
| D | LYS617 |
