Dimeristion domain from human TRF2. Determined by X-ray diffraction at 2.2 Å resolution. Released 5 Sept 2001.
Explore 1H6P in 3D Show helices and sheets RCSB PDB PDBe
1H6P contains 20 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 44-69 | 26 | |
| α-helix | 73-86 | 14 | |
| α-helix | 98-111 | 14 | |
| α-helix | 128-142 | 15 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-181 | 11 | |
| α-helix | 193-201 | 9 | |
| α-helix | 214-227 | 14 | |
| α-helix | 232-234 | 3 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1046-1069 | 24 | |
| α-helix | 1073-1086 | 14 | |
| α-helix | 1097-1112 | 16 | |
| α-helix | 1128-1142 | 15 | |
| α-helix | 1147-1167 | 21 | |
| α-helix | 1171-1180 | 10 | |
| α-helix | 1193-1201 | 9 | |
| α-helix | 1214-1226 | 13 | |
| α-helix | 1232-1234 | 3 | |
| α-helix | 1235-1242 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomeric repeat binding factor 2 | A, B | protein | 203 | HOMO SAPIENS | Q15554 (AlphaFold model) |
>1H6P_1 TELOMERIC REPEAT BINDING FACTOR 2 (chains A, B) AGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLR VMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAV IICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKML RFLESHLDDAEPYLLTMAKKALK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Structure of the Trfh Dimerization Domain of the Human Telomere Proteins Trf1 and Trf2. Fairall, L., Chapman, L., Moss, H. et al. Mol Cell (2001) 8:351-361. DOI 10.1016/S1097-2765(01)00321-5 · PubMed
Other PDB entries of the same protein (UniProt Q15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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