Structures and chemical shift assignments for the ADD domain of the ATRX protein. Determined by solution NMR. Released 26 Jun 2007.
Explore 2JM1 in 3D Show helices and sheets RCSB PDB PDBe
2JM1 contains 4 α-helices and 8 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 |
|---|---|---|---|
| β-strand | 171 | 1 | 1 |
| β-strand | 176 | 1 | 1 |
| β-strand | 187-188 | 2 | 2 |
| β-strand | 195-196 | 2 | 2 |
| α-helix | 198-206 | 9 | |
| β-strand | 212 | 1 | 3 |
| β-strand | 216 | 1 | 3 |
| β-strand | 229-231 | 3 | 4 |
| β-strand | 238-240 | 3 | 4 |
| α-helix | 241-248 | 8 | |
| α-helix | 251-256 | 6 | |
| α-helix | 274-291 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional regulator ATRX | A | protein | 141 | Homo sapiens | P46100 (AlphaFold model) |
>2JM1_1 Transcriptional regulator ATRX (chains A) GAMKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDG MDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLD LVTACNSVFENLEQLLQQNKK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX. Argentaro, A., Yang, J.C., Chapman, L. et al. Proc Natl Acad Sci U S A (2007) 104:11939-11944. DOI 10.1073/pnas.0704057104 · PubMed
Other PDB entries of the same protein (UniProt P46100 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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