5WQD: TRF2 TRFH
Crystal structure of TRF2 TRFH in complex with an NBS1 peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 8 Mar 2017.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organism
- Homo sapiens
- Chains
- 14
- Atoms
- 11,619
- Mol. weight
- 179.21 kDa
- Released
- 8 Mar 2017
Explore 5WQD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5WQD contains 82 α-helices and 14 β-strands across 13 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.
Chain A: 11 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-69 | 25 | |
| α-helix | 73-87 | 15 | |
| α-helix | 95-111 | 17 | |
| β-strand | 118-119 | 2 | 1 |
| α-helix | 128-142 | 15 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-180 | 10 | |
| α-helix | 186-201 | 16 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-227 | 14 | |
| α-helix | 232-234 | 3 | |
| α-helix | 235-243 | 9 | |
Chain B: 12 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 46-69 | 24 | |
| α-helix | 73-87 | 15 | |
| α-helix | 96-111 | 16 | |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 128-142 | 15 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-181 | 11 | |
| α-helix | 186-188 | 3 | |
| α-helix | 189-201 | 13 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-227 | 14 | |
| α-helix | 232-234 | 3 | |
| α-helix | 235-242 | 8 | |
Chain C: 10 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 44-69 | 26 | |
| α-helix | 73-86 | 14 | |
| α-helix | 95-111 | 17 | |
| β-strand | 118-119 | 2 | 3 |
| α-helix | 128-143 | 16 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-181 | 11 | |
| α-helix | 186-201 | 16 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-226 | 13 | |
| α-helix | 235-243 | 9 | |
Chain D: 12 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 44-69 | 26 | |
| α-helix | 73-84 | 12 | |
| α-helix | 96-111 | 16 | |
| β-strand | 118-119 | 2 | 4 |
| β-strand | 121 | 1 | 5 |
| β-strand | 126 | 1 | 5 |
| α-helix | 128-142 | 15 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-182 | 12 | |
| α-helix | 186-201 | 16 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-225 | 12 | |
| α-helix | 226-228 | 3 | |
| α-helix | 232-234 | 3 | |
| α-helix | 235-243 | 9 | |
Chain E: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 49-69 | 21 | |
| α-helix | 73-87 | 15 | |
| α-helix | 95-111 | 17 | |
| α-helix | 122-124 | 3 | |
| α-helix | 128-142 | 15 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-181 | 11 | |
| α-helix | 189-201 | 13 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-226 | 13 | |
| α-helix | 232-234 | 3 | |
| α-helix | 236-242 | 7 | |
Chain F: 13 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-69 | 25 | |
| α-helix | 73-86 | 14 | |
| α-helix | 95-111 | 17 | |
| α-helix | 112-114 | 3 | |
| β-strand | 119 | 1 | 6 |
| α-helix | 128-142 | 15 | |
| α-helix | 147-167 | 21 | |
| α-helix | 171-175 | 5 | |
| α-helix | 192-201 | 10 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-225 | 12 | |
| α-helix | 226-228 | 3 | |
| α-helix | 232-234 | 3 | |
| α-helix | 235-242 | 8 | |
Chain G: 12 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 50-69 | 20 | |
| α-helix | 73-86 | 14 | |
| α-helix | 96-111 | 16 | |
| β-strand | 119 | 1 | 7 |
| α-helix | 128-142 | 15 | |
| α-helix | 147-150 | 4 | |
| α-helix | 154-167 | 14 | |
| α-helix | 171-180 | 10 | |
| α-helix | 188-201 | 14 | |
| α-helix | 207-210 | 4 | |
| α-helix | 214-227 | 14 | |
| α-helix | 232-234 | 3 | |
| α-helix | 237-239 | 3 | |
Chains H, I, J and K: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 434-435 | 2 | 1 |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Telomeric repeat-binding factor 2 | A, B, C, D, E, F, G | protein | 204 | Homo sapiens | Q15554 (AlphaFold model) |
| Nibrin | H, I, J, K, L, M, N | protein | 16 | Homo sapiens | O60934 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>5WQD_1 Telomeric repeat-binding factor 2 (chains A, B, C, D, E, F, G)
GAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLL
RVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAA
VIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKM
LRFLESHLDDAEPYLLTMAKKALK
Sequence of entity 2 (H, I, J, K, L, M, N), FASTA
>5WQD_2 Nibrin (chains H, I, J, K, L, M, N)
KMRIPNYQLSPTKLPS
Primary citation
NBS1 Phosphorylation Status Dictates Repair Choice of Dysfunctional Telomeres. Rai, R., Hu, C., Broton, C. et al. Mol Cell (2017) 65:801-817.e4. DOI 10.1016/j.molcel.2017.01.016 · PubMed
Other PDB entries of the same protein (UniProt Q15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3SJM 1.35 Å, Crystal Structure Analysis of TRF2-Dbd-DNA complex
- 1W0U 1.8 Å, hTRF2 DNA-binding domain in complex with telomeric DNA.
- 3K6G 1.95 Å, Crystal structure of Rap1 and TRF2 complex
- 4M7C 2.05 Å, Crystal structure of the TRF2-binding motif of SLX4 in complex with the TRFH domain of…
- 6J67 2.05 Å, Crystal structure of the compound 34 in a complex with TRF2
- 3BU8 2.15 Å, Crystal Structure of TRF2 TRFH domain and TIN2 peptide complex
- 7C5D 2.15 Å, Crystal structure of TRF2 TRFH domain in complex with a MCPH1 peptide
- 1H6P 2.2 Å, Dimeristion domain from human TRF2
- 5XYF 2.2 Å, Crystal structure of the human TIN2-TPP1-TRF2 telomeric complex
- 4RQI 2.44 Å, Structure of TRF2/RAP1 secondary interaction binding site
- 3BUA 2.5 Å, Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex
- 9Q9K 2.59 Å, Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor…
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