3K6G: Rap1 and TRF2 complex
Crystal structure of Rap1 and TRF2 complex. Determined by X-ray diffraction at 1.95 Å resolution. Released 13 Oct 2010.
- Method
- X-ray diffraction
- Resolution
- 1.95 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 3,184
- Mol. weight
- 50.18 kDa
- Released
- 13 Oct 2010
Explore 3K6G in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3K6G contains 29 α-helices and 4 β-strands across 6 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: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 308-324 | 17 | |
| α-helix | 329-338 | 10 | |
| α-helix | 343-352 | 10 | |
| α-helix | 360-362 | 3 | |
| α-helix | 364-370 | 7 | |
| α-helix | 375-385 | 11 | |
| α-helix | 387-397 | 11 | |
Chain B: 7 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 308-325 | 18 | |
| α-helix | 329-338 | 10 | |
| β-strand | 342 | 1 | 1 |
| α-helix | 343-352 | 10 | |
| α-helix | 359-362 | 4 | |
| α-helix | 364-371 | 8 | |
| α-helix | 375-385 | 11 | |
| α-helix | 387-397 | 11 | |
Chain C: 7 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 308-325 | 18 | |
| α-helix | 329-338 | 10 | |
| β-strand | 342 | 1 | 2 |
| α-helix | 343-352 | 10 | |
| α-helix | 359-362 | 4 | |
| α-helix | 364-370 | 7 | |
| α-helix | 375-385 | 11 | |
| α-helix | 387-397 | 11 | |
Chain D: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 285-296 | 12 | |
| α-helix | 301-310 | 10 | |
| α-helix | 312-313 | 2 | |
Chain E: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 282 | 1 | 1 |
| α-helix | 285-295 | 11 | |
| α-helix | 301-310 | 10 | |
| α-helix | 312-313 | 2 | |
Chain F: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 282 | 1 | 2 |
| α-helix | 285-295 | 11 | |
| α-helix | 301-310 | 10 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Telomeric repeat-binding factor 2-interacting protein 1 | A, B, C | protein | 111 | Homo sapiens | Q9NYB0 (AlphaFold model) |
| Telomeric repeat-binding factor 2 | D, E, F | protein | 42 | Homo sapiens | Q15554 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>3K6G_1 Telomeric repeat-binding factor 2-interacting protein 1 (chains A, B, C)
SEEKVSQPEVGAAIKIIRQLMEKFNLDLSTVTQAFLKNSGELEATSAFLASGQRADGYPI
WSRQDDIDLQKDDEDTREALVKKFGAQNVARRIEFRKKGGSGGSGGSGGKL
Sequence of entity 2 (D, E, F), FASTA
>3K6G_2 Telomeric repeat-binding factor 2 (chains D, E, F)
QLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLP
Primary citation
A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Chen, Y., Rai, R., Zhou, Z.R. et al. Nat Struct Mol Biol (2011) 18:213-221. DOI 10.1038/nsmb.1974 · PubMed
Other PDB entries of the same protein (UniProt Q9NYB0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4RQI 2.44 Å, Structure of TRF2/RAP1 secondary interaction binding site
- 8RD4 3.58 Å, Telomeric RAP1:DNA-PK complex
- 1FEX Solution structure of myb-domain of human RAP1
- 7OZ0 Solution structure of the N-terminal domain of human telomeric Repeat-binding factor…
Browse structure collections
About this viewer
MolViewer shows 3K6G directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.