8EIH
Cryo-EM structure of human DNMT3B homo-tetramer (form I)
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 |
E | 0008168 | molecular_function | methyltransferase activity |
E | 0009008 | molecular_function | DNA-methyltransferase activity |
E | 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 | 150 |
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 | |
E | GLY434-GLU464 |
site_id | SWS_FT_FI2 |
Number of Residues | 280 |
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 | |
E | GLN475-ARG531 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
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 | |
E | CYS651 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Y6K1 |
Chain | Residue | Details |
A | ASP582 | |
C | GLU605 | |
C | ASP627 | |
C | ARG832 | |
D | ASP582 | |
D | GLU605 | |
D | ASP627 | |
D | ARG832 | |
E | ASP582 | |
E | GLU605 | |
E | ASP627 | |
A | GLU605 | |
E | ARG832 | |
A | ASP627 | |
A | ARG832 | |
B | ASP582 | |
B | GLU605 | |
B | ASP627 | |
B | ARG832 | |
C | ASP582 |
site_id | SWS_FT_FI5 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER209 | |
B | SER209 | |
C | SER209 | |
D | SER209 | |
E | SER209 |
site_id | SWS_FT_FI6 |
Number of Residues | 5 |
Details | MOD_RES: Citrulline => ECO:0000250 |
Chain | Residue | Details |
A | ARG410 | |
B | ARG410 | |
C | ARG410 | |
D | ARG410 | |
E | ARG410 |
site_id | SWS_FT_FI7 |
Number of Residues | 10 |
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 | |
E | LYS617 |