Structure and function of the Rad9-binding region of the DNA damage checkpoint adaptor TopBP1. Determined by X-ray diffraction at 2.6 Å resolution. Released 1 Sept 2010.
Explore 2XNK in 3D Show helices and sheets RCSB PDB PDBe
2XNK contains 64 α-helices and 60 β-strands across 4 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 | 7-8 | 2 | |
| β-strand | 11-14 | 4 | 1 |
| α-helix | 21-30 | 10 | |
| α-helix | 36-38 | 3 | |
| β-strand | 39-42 | 4 | 1 |
| α-helix | 44-49 | 6 | |
| β-strand | 57-59 | 3 | 1 |
| α-helix | 66-74 | 9 | |
| β-strand | 78-79 | 2 | 1 |
| α-helix | 81-89 | 9 | |
| α-helix | 93-96 | 4 | |
| β-strand | 101 | 1 | 1 |
| β-strand | 110-114 | 5 | 2 |
| α-helix | 118-130 | 13 | |
| β-strand | 134-135 | 2 | 2 |
| β-strand | 145-148 | 4 | 2 |
| α-helix | 154-161 | 8 | |
| β-strand | 166-167 | 2 | 2 |
| α-helix | 170-180 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 196 | 1 | 2 |
| α-helix | 197-198 | 2 | |
| β-strand | 204-207 | 4 | 3 |
| α-helix | 212-224 | 13 | |
| β-strand | 228-229 | 2 | 3 |
| β-strand | 240-242 | 3 | 3 |
| α-helix | 249-256 | 8 | |
| β-strand | 260-262 | 3 | 3 |
| α-helix | 264-273 | 10 | |
| α-helix | 279-282 | 4 | |
| β-strand | 283 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-14 | 4 | 4 |
| α-helix | 21-33 | 13 | |
| α-helix | 36-38 | 3 | |
| β-strand | 39-42 | 4 | 4 |
| α-helix | 44-49 | 6 | |
| α-helix | 56 | 1 | |
| β-strand | 57-59 | 3 | 4 |
| α-helix | 66-74 | 9 | |
| β-strand | 77-79 | 3 | 4 |
| α-helix | 81-90 | 10 | |
| α-helix | 93-96 | 4 | |
| β-strand | 101 | 1 | 4 |
| β-strand | 110-114 | 5 | 5 |
| α-helix | 118-130 | 13 | |
| β-strand | 134-135 | 2 | 5 |
| β-strand | 145-148 | 4 | 5 |
| α-helix | 154-161 | 8 | |
| β-strand | 166-167 | 2 | 5 |
| α-helix | 170-180 | 11 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196 | 1 | 5 |
| α-helix | 197-198 | 2 | |
| β-strand | 204-207 | 4 | 6 |
| α-helix | 212-224 | 13 | |
| β-strand | 228-229 | 2 | 6 |
| β-strand | 240-242 | 3 | 6 |
| α-helix | 249-256 | 8 | |
| β-strand | 260-262 | 3 | 6 |
| α-helix | 264-273 | 10 | |
| α-helix | 279-282 | 4 | |
| β-strand | 283 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-14 | 4 | 7 |
| α-helix | 21-33 | 13 | |
| α-helix | 36-38 | 3 | |
| β-strand | 39-42 | 4 | 7 |
| α-helix | 44-49 | 6 | |
| β-strand | 57-60 | 4 | 7 |
| α-helix | 66-74 | 9 | |
| β-strand | 77-79 | 3 | 7 |
| α-helix | 81-89 | 9 | |
| α-helix | 93-95 | 3 | |
| β-strand | 101 | 1 | 7 |
| β-strand | 110-114 | 5 | 8 |
| α-helix | 118-129 | 12 | |
| β-strand | 134-135 | 2 | 8 |
| β-strand | 145-148 | 4 | 8 |
| α-helix | 154-161 | 8 | |
| β-strand | 166-167 | 2 | 8 |
| α-helix | 170-180 | 11 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196 | 1 | 8 |
| α-helix | 197-198 | 2 | |
| β-strand | 204-208 | 5 | 9 |
| α-helix | 212-224 | 13 | |
| β-strand | 228-229 | 2 | 9 |
| β-strand | 240-243 | 4 | 9 |
| α-helix | 249-254 | 6 | |
| β-strand | 260-262 | 3 | 9 |
| α-helix | 264-273 | 10 | |
| α-helix | 279-281 | 3 | |
| β-strand | 283 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-14 | 4 | 10 |
| α-helix | 21-30 | 10 | |
| α-helix | 31-33 | 3 | |
| β-strand | 40-42 | 3 | 10 |
| α-helix | 44-49 | 6 | |
| β-strand | 57-59 | 3 | 10 |
| α-helix | 66-73 | 8 | |
| β-strand | 77-79 | 3 | 10 |
| α-helix | 81-89 | 9 | |
| α-helix | 93-96 | 4 | |
| β-strand | 101 | 1 | 10 |
| β-strand | 110-114 | 5 | 11 |
| α-helix | 118-130 | 13 | |
| β-strand | 134-135 | 2 | 11 |
| β-strand | 145-148 | 4 | 11 |
| α-helix | 154-161 | 8 | |
| β-strand | 166-167 | 2 | 11 |
| α-helix | 170-180 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 196 | 1 | 11 |
| β-strand | 204-208 | 5 | 12 |
| α-helix | 212-224 | 13 | |
| β-strand | 228-229 | 2 | 12 |
| β-strand | 240-243 | 4 | 12 |
| α-helix | 249-256 | 8 | |
| β-strand | 260-262 | 3 | 12 |
| α-helix | 264-273 | 10 | |
| α-helix | 276-278 | 3 | |
| α-helix | 279-282 | 4 | |
| β-strand | 283 | 1 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA topoisomerase 2-binding protein 1 | A, B, C, D | protein | 292 | HOMO SAPIENS | Q92547 (AlphaFold model) |
>2XNK_1 DNA TOPOISOMERASE 2-BINDING PROTEIN 1 (chains A, B, C, D) GPMSRNDKEPFFVKFLKSSDNSKCFFKALESIKEFQSEEYLQIITEEEALKIKENDRSLY ICDPFSGVVFDHLKKLGCRIVGPQVVIFCMHHQRCVPRAEHPVYNMVMSDVTISCTSLEK EKREEVHKYVQMMGGRVYRDLNVSVTHLIAGEVGSKKYLVAANLKKPILLPSWIKTLWEK SQEKKITRYTDINMEDFKCPIFLGCIICVTGLCGLDRKEVQQLTVKHGGQYMGQLKMNEC THLIVQEPKGQKYECAKRWNVHCVTTQWFFDSIEKGFCQDESIYKTEPRPEA
Structure and Function of the Rad9-Binding Region of the DNA-Damage Checkpoint Adaptor Topbp1. Rappas, M., Oliver, A.W., Pearl, L.H. Nucleic Acids Res (2011) 39:313. DOI 10.1093/NAR/GKQ743 · PubMed
Other PDB entries of the same protein (UniProt Q92547 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2XNK 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.