Crystal structure of the DNMT3A ADD domain. Determined by X-ray diffraction at 1.45 Å resolution. Released 23 Nov 2022.
Explore 8BA5 in 3D Show helices and sheets RCSB PDB PDBe
8BA5 contains 7 α-helices and 11 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 475-484 | 10 | |
| α-helix | 490-492 | 3 | |
| β-strand | 494 | 1 | 1 |
| β-strand | 502-505 | 4 | 1 |
| β-strand | 509 | 1 | 2 |
| β-strand | 512-514 | 3 | 1 |
| α-helix | 515-524 | 10 | |
| β-strand | 528 | 1 | 3 |
| β-strand | 534 | 1 | 3 |
| β-strand | 546-548 | 3 | 4 |
| β-strand | 557-559 | 3 | 4 |
| α-helix | 560-562 | 3 | |
| α-helix | 563-567 | 5 | |
| α-helix | 571-575 | 5 | |
| β-strand | 591-592 | 2 | 5 |
| β-strand | 595-596 | 2 | 5 |
| β-strand | 597 | 1 | 2 |
| α-helix | 601-608 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA (cytosine-5)-methyltransferase 3A | A | protein | 144 | Homo sapiens | Q9Y6K1 (AlphaFold model) |
>8BA5_1 DNA (cytosine-5)-methyltransferase 3A (chains A) GPLGSRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDD DGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKG TYGLLRRREDWPSRLQMFFANNHD
Water and common crystallization additives (EDO) are not listed.
The MECP2-TRD domain interacts with the DNMT3A-ADD domain at the H3-tail binding site. Kunert, S., Linhard, V., Weirich, S. et al. Protein Sci (2023) 32:e4542-e4542. DOI 10.1002/pro.4542 · PubMed
Other PDB entries of the same protein (UniProt Q9Y6K1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8BA5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.