Crystal Structure of Yeast Rtt107. Determined by X-ray diffraction at 2.31 Å resolution. Released 14 Aug 2019.
Explore 6J0V in 3D Show helices and sheets RCSB PDB PDBe
6J0V contains 59 α-helices and 40 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 |
|---|---|---|---|
| β-strand | 12-16 | 5 | 1 |
| α-helix | 19-21 | 3 | |
| α-helix | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 1 |
| α-helix | 57-64 | 8 | |
| α-helix | 68-69 | 2 | |
| β-strand | 71-73 | 3 | 1 |
| α-helix | 82-83 | 2 | |
| α-helix | 84-88 | 5 | |
| β-strand | 93-94 | 2 | 1 |
| α-helix | 96-105 | 10 | |
| α-helix | 112-114 | 3 | |
| β-strand | 126-129 | 4 | 2 |
| α-helix | 136-148 | 13 | |
| β-strand | 152-154 | 3 | 2 |
| β-strand | 163-165 | 3 | 2 |
| α-helix | 172-177 | 6 | |
| β-strand | 202-204 | 3 | 2 |
| α-helix | 207-215 | 9 | |
| α-helix | 222-226 | 5 | |
| β-strand | 228 | 1 | 2 |
| α-helix | 237-243 | 7 | |
| α-helix | 244-248 | 5 | |
| α-helix | 257-259 | 3 | |
| β-strand | 270-273 | 4 | 3 |
| α-helix | 274 | 1 | |
| α-helix | 281-293 | 13 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 307-313 | 7 | |
| β-strand | 319-321 | 3 | 3 |
| β-strand | 324 | 1 | 4 |
| α-helix | 328-336 | 9 | |
| β-strand | 341-343 | 3 | 3 |
| α-helix | 345-354 | 10 | |
| α-helix | 360-362 | 3 | |
| α-helix | 365-367 | 3 | |
| α-helix | 369 | 1 | |
| β-strand | 370 | 1 | 4 |
| α-helix | 371-373 | 3 | |
| β-strand | 381-385 | 5 | 5 |
| α-helix | 390-402 | 13 | |
| β-strand | 405-407 | 3 | 5 |
| β-strand | 416-419 | 4 | 5 |
| α-helix | 425-434 | 10 | |
| β-strand | 442-444 | 3 | 5 |
| α-helix | 446-455 | 10 | |
| α-helix | 464-466 | 3 | |
| α-helix | 471-473 | 3 | |
| α-helix | 475-477 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 6 |
| β-strand | 11-16 | 6 | 7 |
| α-helix | 19-21 | 3 | |
| α-helix | 22-34 | 13 | |
| β-strand | 37 | 1 | 6 |
| β-strand | 39-44 | 6 | 7 |
| α-helix | 57-64 | 8 | |
| α-helix | 68-69 | 2 | |
| β-strand | 71-73 | 3 | 7 |
| α-helix | 82-83 | 2 | |
| α-helix | 84-88 | 5 | |
| β-strand | 93-94 | 2 | 7 |
| α-helix | 97-105 | 9 | |
| α-helix | 112-114 | 3 | |
| β-strand | 126-129 | 4 | 8 |
| α-helix | 131-133 | 3 | |
| α-helix | 136-148 | 13 | |
| β-strand | 152-154 | 3 | 8 |
| β-strand | 163-165 | 3 | 8 |
| α-helix | 173-177 | 5 | |
| β-strand | 202-204 | 3 | 8 |
| α-helix | 207-215 | 9 | |
| β-strand | 228 | 1 | 8 |
| α-helix | 236-243 | 8 | |
| α-helix | 244-248 | 5 | |
| β-strand | 270-273 | 4 | 9 |
| α-helix | 274 | 1 | |
| α-helix | 281-293 | 13 | |
| β-strand | 297-300 | 4 | 9 |
| α-helix | 307-313 | 7 | |
| β-strand | 317-321 | 5 | 9 |
| β-strand | 324 | 1 | 10 |
| α-helix | 328-336 | 9 | |
| β-strand | 341-343 | 3 | 9 |
| α-helix | 345-354 | 10 | |
| α-helix | 360-362 | 3 | |
| α-helix | 365-367 | 3 | |
| α-helix | 369 | 1 | |
| β-strand | 370 | 1 | 10 |
| α-helix | 371-373 | 3 | |
| β-strand | 381-385 | 5 | 11 |
| α-helix | 390-402 | 13 | |
| β-strand | 405-406 | 2 | 11 |
| β-strand | 416-419 | 4 | 11 |
| α-helix | 424-435 | 12 | |
| β-strand | 442-444 | 3 | 11 |
| α-helix | 446-454 | 9 | |
| α-helix | 464-466 | 3 | |
| α-helix | 471-473 | 3 | |
| α-helix | 475-477 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulator of Ty1 transposition protein 107 | A, B | protein | 513 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P38850 (AlphaFold model) |
>6J0V_1 Regulator of Ty1 transposition protein 107 (chains A, B) MSTSLLFEQLNFLILVAAEAELPIAHSTRKLLMDNSCNNCQIYELYNENLKDVKTDKDWF MNKFGPQTVHFVISNTINFPFYKIVYFDLLIPVVSHTWVQDSVKTKRHLRTNMYSPNPFH LLRDCQVYISKSSFNKCEYILYSDLLHLLGGTLVNYISNRTTHVIVQSPQDPIIATVSKL TFGSFSSSSTNKHTEKPLREWKFVYPIWILYHFKMAKPLKGELATLCELDMQDTSEEQLF AKWEEVIGDKQTSSSQLTLHPNKTLFKNHHFAISPDLNFFTPLYWFLKGFIEDLDGKVTP LSFSDDLKSVYQAFPDIDCYIGHSANSPILEKTKSIKPEIHVGNVSWLFYMFALQKFTPV SQCKLIHQPFHAKLFTSKELTVAYTNYFGSQRFYIQRLVEILGGLSTPELTRKNTHLITK STIGKKFKVAKKWSLDPQNAIIVTNHMWLEQCYMNNSKLNPKDSRFQNFKLDDNMGWNIG QIGMDHSSLPTPKNLSMVTYDTQSISEKPPPTN
Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107. Wan, B., Wu, J., Meng, X. et al. Mol Cell (2019) 75:238-251.e5. DOI 10.1016/j.molcel.2019.05.035 · PubMed
Other PDB entries of the same protein (UniProt P38850 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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