Structures and chemical shift assignments for the ADD domain of the ATRX protein. Determined by solution NMR. Released 8 Jun 2011.
Explore 2LD1 in 3D Show helices and sheets RCSB PDB PDBe
2LD1 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 | 170-171 | 2 | 1 |
| β-strand | 176-177 | 2 | 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 | 274-292 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional regulator ATRX | A | protein | 142 | Homo sapiens | P46100 (AlphaFold model) |
>2LD1_1 Transcriptional regulator ATRX (chains A) GAMADKRGDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSD GMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLL DLVTACNSVFENLEQLLQQNKK
| 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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