Crystal structure of activated Notch, CSL and MAML on HES-1 promoter DNA sequence. Determined by X-ray diffraction at 3.25 Å resolution. Released 4 Apr 2006.
Explore 2F8X in 3D Show helices and sheets RCSB PDB PDBe
2F8X contains 28 α-helices and 51 β-strands across 3 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 | 12-14 | 3 | |
| α-helix | 16-18 | 3 | |
| α-helix | 19-27 | 9 | |
| β-strand | 32-33 | 2 | 1 |
| β-strand | 36-39 | 4 | 2 |
| β-strand | 41-43 | 3 | 3 |
| β-strand | 45 | 1 | 4 |
| β-strand | 58-59 | 2 | 2 |
| β-strand | 62 | 1 | 1 |
| α-helix | 65-74 | 10 | |
| β-strand | 88-91 | 4 | 5 |
| α-helix | 98 | 1 | |
| β-strand | 99-100 | 2 | 5 |
| β-strand | 110 | 1 | 2 |
| β-strand | 117 | 1 | 4 |
| β-strand | 124-125 | 2 | 3 |
| β-strand | 127-132 | 6 | 5 |
| β-strand | 138-143 | 6 | 5 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-150 | 4 | 3 |
| β-strand | 166 | 1 | 6 |
| β-strand | 168 | 1 | 7 |
| β-strand | 172-177 | 6 | 2 |
| α-helix | 179-181 | 3 | |
| β-strand | 187-188 | 2 | 2 |
| β-strand | 190-192 | 3 | 8 |
| β-strand | 195-197 | 3 | 8 |
| β-strand | 206-211 | 6 | 2 |
| β-strand | 227 | 1 | 7 |
| β-strand | 229 | 1 | 9 |
| β-strand | 233-238 | 6 | 2 |
| β-strand | 244 | 1 | 2 |
| β-strand | 248-252 | 5 | 2 |
| β-strand | 253-254 | 2 | 10 |
| β-strand | 257-259 | 3 | 10 |
| β-strand | 265 | 1 | 9 |
| β-strand | 267 | 1 | 6 |
| β-strand | 270-275 | 6 | 2 |
| β-strand | 283 | 1 | 2 |
| β-strand | 285-286 | 2 | 11 |
| β-strand | 291-292 | 2 | 11 |
| β-strand | 300 | 1 | 12 |
| β-strand | 302 | 1 | 12 |
| β-strand | 305-307 | 3 | 10 |
| β-strand | 314-322 | 9 | 2 |
| β-strand | 325-326 | 2 | 1 |
| β-strand | 329 | 1 | 13 |
| β-strand | 331 | 1 | 13 |
| α-helix | 338 | 1 | |
| α-helix | 340 | 1 | |
| β-strand | 342-348 | 7 | 14 |
| α-helix | 352-354 | 3 | |
| β-strand | 356-362 | 7 | 14 |
| β-strand | 368-372 | 5 | 15 |
| β-strand | 375-377 | 3 | 15 |
| β-strand | 379-383 | 5 | 14 |
| β-strand | 386-390 | 5 | 14 |
| α-helix | 391-393 | 3 | |
| α-helix | 394-397 | 4 | |
| β-strand | 408-409 | 2 | 16 |
| β-strand | 412-416 | 5 | 15 |
| β-strand | 421-423 | 3 | 15 |
| β-strand | 429-430 | 2 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1885-1891 | 7 | |
| α-helix | 1910-1915 | 6 | |
| α-helix | 1923-1925 | 3 | |
| α-helix | 1932-1938 | 7 | |
| α-helix | 1942-1950 | 9 | |
| α-helix | 1965-1971 | 7 | |
| α-helix | 1975-1983 | 9 | |
| α-helix | 1999-2005 | 7 | |
| α-helix | 2011-2017 | 7 | |
| α-helix | 2032-2038 | 7 | |
| α-helix | 2042-2050 | 9 | |
| α-helix | 2065-2072 | 8 | |
| α-helix | 2075-2083 | 9 | |
| α-helix | 2098-2104 | 7 | |
| α-helix | 2108-2116 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-69 | 53 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(*gp*tp*tp*ap*cp*tp*gp*tp*gp*gp*gp*ap*ap*ap*gp*ap*ap*a)-3' | X | DNA | 18 | ||
| 5'-d(*tp*tp*tp*cp*tp*tp*tp*cp*cp*cp*ap*cp*ap*gp*tp*ap*ap*c)-3' | Y | DNA | 18 | ||
| Recombining binding protein suppressor of hairless, isoform 4 | C | protein | 434 | Homo sapiens | Q06330 (AlphaFold model) |
| Neurogenic locus notch homolog protein 1 | K | protein | 256 | Homo sapiens | P46531 (AlphaFold model) |
| Mastermind-like protein 1 | M | protein | 63 | Homo sapiens | Q92585 (AlphaFold model) |
>2F8X_1 5'-D(*GP*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*AP*AP*A)-3' (chains X) GTTACTGTGGGAAAGAAA
>2F8X_2 5'-D(*TP*TP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*TP*AP*AP*C)-3' (chains Y) TTTCTTTCCCACAGTAAC
>2F8X_3 Recombining binding protein suppressor of hairless, isoform 4 (chains C) MGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWK KKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFML SVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTR YLHVEGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPR LIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEM INDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPN LRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLT FTYTPEPGHHHHHH
>2F8X_4 Neurogenic locus notch homolog protein 1 (chains K) GMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGET ALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDA RMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKN GANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIV RLLDEYNLVRSPQLHG
>2F8X_5 Mastermind-like protein 1 (chains M) GLPRHSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQAKAKRA GKH
Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Nam, Y., Sliz, P., Song, L. et al. Cell (2006) 124:973-983. DOI 10.1016/j.cell.2005.12.037 · PubMed
Other PDB entries of the same protein (UniProt Q06330 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2F8X 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.