Cryo-EM structure of TELO2-TTI1-TTI2 complex. Determined by electron microscopy at 4.2 Å resolution. Released 22 Jun 2022.
Explore 7F4U in 3D Show helices and sheets RCSB PDB PDBe
7F4U contains 77 α-helices and 0 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 | 8-20 | 13 | |
| α-helix | 25-37 | 13 | |
| α-helix | 49-52 | 4 | |
| α-helix | 53-58 | 6 | |
| α-helix | 59-64 | 6 | |
| α-helix | 65-69 | 5 | |
| α-helix | 74-77 | 4 | |
| α-helix | 83-92 | 10 | |
| α-helix | 97-109 | 13 | |
| α-helix | 117-129 | 13 | |
| α-helix | 137-139 | 3 | |
| α-helix | 146-166 | 21 | |
| α-helix | 170-175 | 6 | |
| α-helix | 184-202 | 19 | |
| α-helix | 209-224 | 16 | |
| α-helix | 231-242 | 12 | |
| α-helix | 246-257 | 12 | |
| α-helix | 266-273 | 8 | |
| α-helix | 278-285 | 8 | |
| α-helix | 294-305 | 12 | |
| α-helix | 314-325 | 12 | |
| α-helix | 332-348 | 17 | |
| α-helix | 351-353 | 3 | |
| α-helix | 354-369 | 16 | |
| α-helix | 379-394 | 16 | |
| α-helix | 400-415 | 16 | |
| α-helix | 422-429 | 8 | |
| α-helix | 443-448 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 167-184 | 18 | |
| α-helix | 194-198 | 5 | |
| α-helix | 199-207 | 9 | |
| α-helix | 214-221 | 8 | |
| α-helix | 235-260 | 26 | |
| α-helix | 266-279 | 14 | |
| α-helix | 289-300 | 12 | |
| α-helix | 302-304 | 3 | |
| α-helix | 310-324 | 15 | |
| α-helix | 332-340 | 9 | |
| α-helix | 349-358 | 10 | |
| α-helix | 369-384 | 16 | |
| α-helix | 386-389 | 4 | |
| α-helix | 397-410 | 14 | |
| α-helix | 416-419 | 4 | |
| α-helix | 422-435 | 14 | |
| α-helix | 484-494 | 11 | |
| α-helix | 502-514 | 13 | |
| α-helix | 519-534 | 16 | |
| α-helix | 550-567 | 18 | |
| α-helix | 617-640 | 24 | |
| α-helix | 644-646 | 3 | |
| α-helix | 649-659 | 11 | |
| α-helix | 664-668 | 5 | |
| α-helix | 669-682 | 14 | |
| α-helix | 688-692 | 5 | |
| α-helix | 696-707 | 12 | |
| α-helix | 716-722 | 7 | |
| α-helix | 728-730 | 3 | |
| α-helix | 731-747 | 17 | |
| α-helix | 752-768 | 17 | |
| α-helix | 769-773 | 5 | |
| α-helix | 858-872 | 15 | |
| α-helix | 879-891 | 13 | |
| α-helix | 899-914 | 16 | |
| α-helix | 925-934 | 10 | |
| α-helix | 940-953 | 14 | |
| α-helix | 978-990 | 13 | |
| α-helix | 996-1002 | 7 | |
| α-helix | 1023-1027 | 5 | |
| α-helix | 1047-1050 | 4 | |
| α-helix | 1060-1066 | 7 | |
| α-helix | 1067-1069 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-47 | 6 | |
| α-helix | 68-75 | 8 | |
| α-helix | 96-110 | 15 | |
| α-helix | 122-130 | 9 | |
| α-helix | 144-162 | 19 | |
| α-helix | 178-187 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomere length regulation protein TEL2 homolog | A | protein | 837 | Homo sapiens | Q9Y4R8 (AlphaFold model) |
| TELO2-interacting protein 1 homolog | B | protein | 1095 | Homo sapiens | O43156 (AlphaFold model) |
| TELO2-interacting protein 2 | C | protein | 508 | Homo sapiens |
>7F4U_1 Telomere length regulation protein TEL2 homolog (chains A) MEPAPSEVRLAVREAIHALSSSEDGGHIFCTLESLKRYLGEMEPPALPREKEEFASAHFS PVLRCLASRLSPAWLELLPHGRLEELWASFFLEGPADQAFLVLMETIEGAAGPSFRLMKM ARLLARFLREGRLAVLMEAQCRQQTQPGFILLRETLLGKVVALPDHLGNRLQQENLAEFF PQNYFRLLGEEVVRVLQAVVDSLQGGLDSSVSFVSQVLGKACVHGRQQEILGVLVPRLAA LTQGSYLHQRVCWRLVEQVPDRAMEAVLTGLVEAALGPEVLSRLLGNLVVKNKKAQFVMT QKLLFLQSRLTTPMLQSLLGHLAMDSQRRPLLLQVLKELLETWGSSSAIRHTPLPQQRHV SKAVLICLAQLGEPELRDSRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVVSARIHPE GPPLKFQYEEDELSLELLALASPQPAGDGASEAGTSLVPATAEPPAETPAEIVDGGVPQA QLAGSDSDLDSDDEFVPYDMSGDRELKSSKAPAYVRDCVEALTTSEDIERWEAALRALEG LVYRSPTATREVSVELAKVLLHLEEKTCVVGFAGLRQRALVAVTVTDPAPVADYLTSQFY ALNYSLRQRMDILDVLTLAAQELSRPGCLGRTPQPGSPSPNTPCLPEAAVSQPGSAVASD WRVVVEERIRSKTQRLSKGGPRQGPAGSPSRFNSVAGHFFFPLLQRFDRPLVTFDLLGED QLVLGRLAHTLGALMCLAVNTTVAVAMGKALLEFVWALRFHIDAYVRQGLLSAVSSVLLS LPAARLLEDLMDELLEARSWLADVAEKDPDEDCRTLALRALLLLQRLKNRLLPPASP
>7F4U_2 TELO2-interacting protein 1 homolog (chains B) MHHHHHMAVFDTPEEAFGVLRPVCVQLTKTQTVENVEHLQTRLQAVSDSALQELQQYILF PLRFTLKTPGPKRERLIQSVVECLTFVLSSTCVKEQELLQELFSELSACLYSPSSQKPAA VSEELKLAVIQGLSTLMHSAYGDIILTFYEPSILPRLGFAVSLLLGLAEQEXXXXXXXXX XXXXXXXXXXXDCQDHPRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGDFKQGHSIVVS SLKIFYKTVSFIMADEQLKRISKVQAKPAVEHRVAELMVYREADWVKKTGDKLTILIKKI IECVSVHPHWKVRLELVELVEDLLLKCSQSLVECAGPLLKALVGLVNDESPEIQAQCNKV LRHFADQKVVVGNKALADILSESLHSLATSLPRLMNSQDDQGKFSTLSLLLGYLKLLGPK INFVLNSVAHLQRLSKALIQVLELDVADIKIVEERRWNSDDLNASPKTSATQPWNRIQRR YFRFFTDERIFMLLRQVCQLLGYYGNLYLLVDHFMELYHQSVVYRKQAAMILNELVTGAA GLEVEDLHEKHIKTNPEELREIVTSILEEYTSQENWYLVTCLETEEMGEELMMEHPGLQA ITSGEHTCQVTSFLAFSKPSPTICSMNSNIWQICIQLEGIGQFAYALGKDFCLLLMSALY PVLEKAGDQTLLISQVATSTMMDVCRACGYDSLQHLINQNSDYLVNGISLNLRHLALHPH TPKVLEVMLRNSDANLLPLVADVVQDVLATLDQFYDKRAASFVSVLHALMAALAQWFPDT GNLGHLQEQSLGEEGSHLNQRPAALEKSTTTAEDIEQFLLNYLKEKDVADGNVSDFDNEE EEQSVPPKVDENDTRPDVEPPLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXXXXRLTRDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX XXXXXLVTQAPISARAGPVYSHXXXXXXXXXXXXXXXXXXXXXXXXXXXLNKVADACLIY LSVKQPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGQQ NPYTTNVLQLLKELQ
>7F4U_3 TELO2-interacting protein 2 (chains C) MELDSALEAPSQEDSNLSEELSHSAFGQAFSKILHCLARPXXXXXXXXDAVLKDLGDLIE ATEFXXXXXXXXXXXXXXXXXXXXVAKALEKYAAXXXXXXXXXXXXXXXXXXXXQVGLLF XXXXXXXXXXXXXLVGPAWQTGLXXXXXXXXXXXXXXXXXXXXXTPRSREVAREXXXXXX XXXXXXXXXXFLHGENEDEKGRLSVILGLLKPDLYKESWKNNPAIKHVFSWTLQQVTRPW LSQHLERVLPASLVISDDYQTENKILGVHCLHHIVLNVPAADLLQYNRAQVLYHAISNHL YTPEHHLIQAVLLCLLDLFPILEKTLHWKGDGARPTTHCDEVLRLILTHMEPEHRLLLRR TYARNLPAFVNRLGILTVRHLKRLERVIIGYLEVYDGPEEEARLKILETLKLLMQHTWPR VSCRLVVLLKALLKLICDVARDPNLTPESVKSALLQEATDCLILLDRCSQGRVKGLLAKI PQSCEDRKVVNYIRKVQQVSEGAPYNGT
Structure of the Human TELO2-TTI1-TTI2 Complex. Kim, Y., Park, J., Joo, S.Y. et al. J Mol Biol (2022) 434:167370-167370. DOI 10.1016/j.jmb.2021.167370 · PubMed
Other PDB entries of the same protein (UniProt Q9Y4R8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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