Crystal structure of ATRX ADD domain in free state. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Jun 2011.
Explore 3QLN in 3D Show helices and sheets RCSB PDB PDBe
3QLN contains 12 α-helices and 16 β-strands across 2 chains. 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 | 1 | 1 |
| β-strand | 177 | 1 | 1 |
| β-strand | 186-188 | 3 | 2 |
| β-strand | 195-197 | 3 | 2 |
| α-helix | 198-205 | 8 | |
| α-helix | 208-210 | 3 | |
| β-strand | 211 | 1 | 3 |
| β-strand | 217 | 1 | 3 |
| β-strand | 229-231 | 3 | 4 |
| β-strand | 238-240 | 3 | 4 |
| α-helix | 241-248 | 8 | |
| α-helix | 250-256 | 7 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-286 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 170 | 1 | 5 |
| β-strand | 177 | 1 | 5 |
| β-strand | 186-188 | 3 | 6 |
| β-strand | 195-197 | 3 | 6 |
| α-helix | 198-205 | 8 | |
| α-helix | 208-210 | 3 | |
| β-strand | 211 | 1 | 7 |
| β-strand | 217 | 1 | 7 |
| β-strand | 229-231 | 3 | 8 |
| β-strand | 238-240 | 3 | 8 |
| α-helix | 241-248 | 8 | |
| α-helix | 250-257 | 8 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-284 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional regulator ATRX | A, B | protein | 129 | Homo sapiens | P46100 (AlphaFold model) |
>3QLN_1 Transcriptional regulator ATRX (chains A, B) GPLGSMGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQC RWCAEGGNLICCDFCHNAFCKKCILRNLGRRELSTIMDENNQWYCYICHPEPLLDLVTAC NSVYENLEQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 6 |
ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome. Iwase, S., Xiang, B., Ghosh, S. et al. Nat Struct Mol Biol (2011) 18:769-776. DOI 10.1038/nsmb.2062 · 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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