Tti1-Telo2 complex. Determined by electron microscopy at 3.83 Å resolution. Released 2 Sept 2026.
Explore 9WJS in 3D Show helices and sheets RCSB PDB PDBe
9WJS contains 67 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 197-222 | 26 | |
| α-helix | 228-247 | 20 | |
| α-helix | 249-254 | 6 | |
| α-helix | 277-300 | 24 | |
| α-helix | 304-341 | 38 | |
| α-helix | 345-361 | 17 | |
| α-helix | 363-366 | 4 | |
| α-helix | 371-391 | 21 | |
| α-helix | 394-420 | 27 | |
| α-helix | 422-436 | 15 | |
| α-helix | 443-445 | 3 | |
| α-helix | 467-472 | 6 | |
| α-helix | 482-498 | 17 | |
| α-helix | 501-514 | 14 | |
| α-helix | 516-534 | 19 | |
| α-helix | 547-549 | 3 | |
| α-helix | 550-565 | 16 | |
| α-helix | 567-570 | 4 | |
| α-helix | 622-641 | 20 | |
| α-helix | 643-661 | 19 | |
| α-helix | 665-682 | 18 | |
| α-helix | 687-707 | 21 | |
| α-helix | 714-725 | 12 | |
| α-helix | 730-770 | 41 | |
| α-helix | 859-875 | 17 | |
| α-helix | 879-898 | 20 | |
| α-helix | 900-920 | 21 | |
| α-helix | 923-940 | 18 | |
| α-helix | 942-947 | 6 | |
| α-helix | 948-952 | 5 | |
| α-helix | 953-969 | 17 | |
| α-helix | 972-976 | 5 | |
| α-helix | 978-997 | 20 | |
| α-helix | 1001-1015 | 15 | |
| α-helix | 1021-1037 | 17 | |
| α-helix | 1039-1048 | 10 | |
| α-helix | 1076-1088 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-21 | 14 | |
| α-helix | 25-39 | 15 | |
| α-helix | 45-47 | 3 | |
| α-helix | 48-53 | 6 | |
| α-helix | 54-59 | 6 | |
| α-helix | 60-69 | 10 | |
| α-helix | 72-77 | 6 | |
| α-helix | 82-93 | 12 | |
| α-helix | 96-109 | 14 | |
| α-helix | 115-130 | 16 | |
| α-helix | 132-141 | 10 | |
| α-helix | 146-149 | 4 | |
| α-helix | 150-171 | 22 | |
| α-helix | 181-205 | 25 | |
| α-helix | 211-224 | 14 | |
| α-helix | 227-244 | 18 | |
| α-helix | 246-258 | 13 | |
| α-helix | 261-274 | 14 | |
| α-helix | 278-285 | 8 | |
| α-helix | 288-291 | 4 | |
| α-helix | 293-297 | 5 | |
| α-helix | 298-306 | 9 | |
| α-helix | 312-324 | 13 | |
| α-helix | 328-344 | 17 | |
| α-helix | 346-351 | 6 | |
| α-helix | 354-370 | 17 | |
| α-helix | 373-396 | 24 | |
| α-helix | 401-417 | 17 | |
| α-helix | 422-423 | 2 | |
| α-helix | 432-441 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tti1 | A | protein | 733 | Homo sapiens | |
| Telomere length regulation protein TEL2 homolog | C | protein | 437 | Homo sapiens | Q9Y4R8 (AlphaFold model) |
>9WJS_1 Tti1 (chains A) ELEQKQLGDLFASFLPGISTALTRLITGDFKQGHSIVVSSLKIFYKTVSFIMADEQLKRI SKMVYREADWVKKTGDKLTILIKKIIECVSVHPHWKVRLELVELVEDLLLKCSQSLVECA GPLLKALVGLVNDESPEIQAQCNKVLRHFADQKVVVGNKALADILSESLHSLATSLPRLM NSQDDQGKFSTLSLLLGYLKLLGPKINFVLNSVAHLQRLSKALIQVLELDVADIKIVEER RWNSDDLNASPKTSATQPWNRIQRRYFRFFTDERIFMLLRQVCQLLGYYGNLYLLVDHFM ELYHQSVVYRKQAAMILNELVTGAAGLEVEDLHEKHIKTNPEELREIVTSILEEYTSQEN WYLVTCNSNIWQICIQLEGIGQFAYALGKDFCLLLMSALYPVLEKAGDQTLLISQVATST MMDVCRACGYDSLQHLINQNSDYLVNGISLNLRHLALHPHTPKVLEVMLRNSDANLLPLV ADVVQDVLATLDQFYDKRAASFVSVLHALMAALAQWFPDLQIQIAMDVMERCIHLLSDKN LQIRLKVLDVLDLCVVVLQSHKNQLLPLAHQAWPSLVHRLTRDAPLAVLRAFKVLRTLGS KCGDFLRSRFCKDVLPKLAGSLVTQAPISARAGPVYSHTLAFKLQLAVLQGLGPLCERLD LGEGDLNKVADACLIYLSVKQPVKLQEAARSVFLHLMKVDPDSTWFLLNELHGASGQQNP YTTNVLQLLKELQ
>9WJS_2 Telomere length regulation protein TEL2 homolog (chains C) EVRLAVREAIHALSSSEDGGHIFCTLESLKRYLGEMEPPALPREKEEFASAHFSPVLRCL ASRLSPAWLELLPHGRLEELWASFFLEGPADQAFLVLMETIEGAAGPSFRLMKMARLLAR FLREGRLAVLMEAQCRQQTQPGFILLRETLLGKVVALPDHLGNRLQQENLAEFFPQNYFR LLGEEVVRVLQAVVDSLQGGLDSSVSFVSQVLGKACVHGRQQEILGVLVPRLAALTQGSY LHQRVCWRLVEQVPDRAMEAVLTGLVEAALGPEVLSRLLGNLVVKNKKAQFVMTQKLLFL QSRLTTPMLQSLLGHLAMDSQRRPLLLQVLKELLETWGSSSAIRHTPLPQQRHVSKAVLI CLAQLGEPELRDSRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVVSARIHPEGPPLKF QYEEDELSLELLALASP
GNB1L Chaperone Activity Licenses SAGA-Mediated Immune Evasion in Tumors. Qin, Y., Xu, G. To be published.
Other PDB entries of the same protein (UniProt Q9Y4R8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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