Cryo-EM map of human telomerase-DNA-TPP1-POT1 complex (sharpened map). Determined by electron microscopy at 3.9 Å resolution. Released 2 Mar 2022.
Explore 7QXB in 3D Show helices and sheets RCSB PDB PDBe
7QXB contains 76 α-helices and 64 β-strands across 5 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 | 8-16 | 9 | |
| β-strand | 20-23 | 4 | 1 |
| α-helix | 24-31 | 8 | |
| α-helix | 33 | 1 | |
| α-helix | 45-52 | 8 | |
| β-strand | 54-58 | 5 | 1 |
| α-helix | 77-90 | 14 | |
| α-helix | 96-98 | 3 | |
| β-strand | 101-103 | 3 | 2 |
| β-strand | 119-121 | 3 | 2 |
| α-helix | 126-132 | 7 | |
| α-helix | 135-144 | 10 | |
| α-helix | 146-154 | 9 | |
| β-strand | 157-161 | 5 | 1 |
| β-strand | 166-169 | 4 | 1 |
| β-strand | 325-327 | 3 | 3 |
| α-helix | 328-331 | 4 | |
| β-strand | 332 | 1 | 4 |
| α-helix | 341-342 | 2 | |
| α-helix | 346-349 | 4 | |
| α-helix | 354-365 | 12 | |
| α-helix | 380-383 | 4 | |
| α-helix | 384-400 | 17 | |
| α-helix | 405-412 | 8 | |
| α-helix | 445-453 | 9 | |
| α-helix | 458-472 | 15 | |
| α-helix | 475-478 | 4 | |
| α-helix | 481-496 | 16 | |
| β-strand | 502-504 | 3 | 3 |
| α-helix | 505-508 | 4 | |
| α-helix | 518-520 | 3 | |
| α-helix | 531-548 | 18 | |
| α-helix | 549-553 | 5 | |
| α-helix | 554-560 | 7 | |
| β-strand | 561-564 | 4 | 4 |
| β-strand | 569 | 1 | 5 |
| β-strand | 571 | 1 | 5 |
| β-strand | 574-577 | 4 | 4 |
| α-helix | 578-595 | 18 | |
| β-strand | 599-600 | 2 | 6 |
| α-helix | 603-611 | 9 | |
| α-helix | 615-616 | 2 | |
| β-strand | 617-626 | 10 | 6 |
| β-strand | 629-636 | 8 | 6 |
| α-helix | 654-671 | 18 | |
| α-helix | 673-676 | 4 | |
| α-helix | 683-687 | 5 | |
| α-helix | 690-698 | 9 | |
| β-strand | 707-712 | 6 | 7 |
| β-strand | 713 | 1 | 8 |
| α-helix | 722-733 | 12 | |
| β-strand | 738-749 | 12 | 1 |
| β-strand | 755-765 | 11 | 1 |
| α-helix | 766-768 | 3 | |
| α-helix | 773-783 | 11 | |
| β-strand | 789-801 | 13 | 1 |
| α-helix | 802-814 | 13 | |
| β-strand | 816-820 | 5 | 6 |
| β-strand | 823-826 | 4 | 6 |
| α-helix | 836-853 | 18 | |
| α-helix | 855-860 | 6 | |
| β-strand | 863-865 | 3 | 7 |
| β-strand | 869-874 | 6 | 7 |
| α-helix | 877-889 | 13 | |
| β-strand | 891 | 1 | 9 |
| β-strand | 896 | 1 | 9 |
| β-strand | 898 | 1 | 8 |
| α-helix | 900-902 | 3 | |
| β-strand | 904-905 | 2 | 7 |
| β-strand | 920-921 | 2 | 7 |
| β-strand | 927-930 | 4 | 10 |
| β-strand | 933-936 | 4 | 10 |
| β-strand | 942-944 | 3 | 10 |
| β-strand | 953 | 1 | 11 |
| α-helix | 966-981 | 16 | |
| α-helix | 984-987 | 4 | |
| α-helix | 994-1017 | 24 | |
| α-helix | 1025-1027 | 3 | |
| α-helix | 1030-1050 | 21 | |
| β-strand | 1058 | 1 | 12 |
| β-strand | 1062 | 1 | 12 |
| α-helix | 1067-1084 | 18 | |
| α-helix | 1086-1106 | 21 | |
| α-helix | 1110-1118 | 9 | |
| α-helix | 1125-1128 | 4 | |
| β-strand | 1131 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| α-helix | 28-37 | 10 | |
| β-strand | 43-44 | 2 | 13 |
| α-helix | 47-72 | 26 | |
| β-strand | 79 | 1 | 14 |
| α-helix | 81-89 | 9 | |
| α-helix | 93-97 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-49 | 11 | |
| β-strand | 55 | 1 | 14 |
| α-helix | 57-85 | 29 | |
| β-strand | 89-90 | 2 | 13 |
| α-helix | 92-102 | 11 | |
| α-helix | 106-123 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 99-103 | 5 | |
| β-strand | 113-123 | 11 | 15 |
| β-strand | 142-147 | 6 | 15 |
| β-strand | 152-157 | 6 | 15 |
| α-helix | 159-164 | 6 | |
| α-helix | 170-172 | 3 | |
| β-strand | 180-187 | 8 | 15 |
| β-strand | 190 | 1 | 16 |
| β-strand | 203 | 1 | 16 |
| β-strand | 204-215 | 12 | 15 |
| α-helix | 217-220 | 4 | |
| β-strand | 223 | 1 | 15 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-237 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-13 | 5 | |
| β-strand | 21-37 | 17 | 17 |
| β-strand | 43-50 | 8 | 17 |
| β-strand | 56-63 | 8 | 17 |
| α-helix | 66-68 | 3 | |
| β-strand | 78-89 | 12 | 17 |
| β-strand | 92-105 | 14 | 17 |
| β-strand | 117 | 1 | 17 |
| α-helix | 153-155 | 3 | |
| β-strand | 161-173 | 13 | 18 |
| β-strand | 178-184 | 7 | 18 |
| α-helix | 192 | 1 | |
| β-strand | 193 | 1 | 19 |
| α-helix | 194 | 1 | |
| β-strand | 204-205 | 2 | 18 |
| α-helix | 207-213 | 7 | |
| α-helix | 214-216 | 3 | |
| β-strand | 218-223 | 6 | 18 |
| α-helix | 226-231 | 6 | |
| α-helix | 233-234 | 2 | |
| β-strand | 238-247 | 10 | 18 |
| β-strand | 261 | 1 | 19 |
| β-strand | 262-265 | 4 | 18 |
| α-helix | 270-272 | 3 | |
| β-strand | 274-278 | 5 | 18 |
| α-helix | 279 | 1 | |
| α-helix | 283-298 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomerase reverse transcriptase | A | protein | 1132 | Homo sapiens | O14746 (AlphaFold model) |
| human telomerase RNA | B | RNA | 451 | Homo sapiens | |
| Histone H2A | L | protein | 130 | Homo sapiens | B2R5B3 (AlphaFold model) |
| Histone H2B | M | protein | 166 | Homo sapiens | B4DR52 (AlphaFold model) |
| Telomeric DNA | N | DNA | 30 | Homo sapiens | |
| Adrenocortical dysplasia homolog (Mouse), isoform CRA_a | O | protein | 458 | Homo sapiens | Q96AP0 (AlphaFold model) |
| Protection of telomeres protein 1 | P | protein | 634 | Homo sapiens | Q9NUX5 |
>7QXB_1 Telomerase reverse transcriptase (chains A) MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPW DARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVR SYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGA ATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRR GAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVG RQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRL VETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVT PAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGS RHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEI LAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRE LSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKA LFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTI PQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHL QETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTL LCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNL RKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTF NRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLP FHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLL KLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD
>7QXB_2 human telomerase RNA (chains B) GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG GACGUGCACCCAGGACUCGGCUCACACAUGC
>7QXB_3 Histone H2A (chains L) MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVRRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK TESHHKAKGK
>7QXB_4 Histone H2B (chains M) MPDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT KYTSSNPRNLSPTKPGGSEDRQPPPSQLSAIPPFCLVLRAGIAGQV
>7QXB_5 Telomeric DNA (chains N) TTAGGGTTAGGGTTAGGGTTAGGGTTAGGG
>7QXB_6 Adrenocortical dysplasia homolog (Mouse), isoform CRA_a (chains O) MAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLV SDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQV DRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSNAGLSLSQLLDEMREDQE HQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCISENDQLILSSL GPCQRTQGPELPPPDPALQDLSLTLIASPPSSPSSSGTPALPGHMSSEESGTSISLLPAL SLAAPDPGQRSSSQPSPAICSAPATLTPRSPHASRTPSSPLQSCTPSLSPRSHVPSPHQA LVTRPQKPSLEFKEFVGLPCKNRPPFPRTGATRGAQEPCSVWEPPKRHRDGSAFQYEYEP PCTSLCARVQAVRLPPQLMAWALHFLMDAQPGSEPTPM
>7QXB_7 Protection of telomeres protein 1 (chains P) MSLVPATNYIYTPLNQLKGGTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQTNVKLTCL LFSGNYEALPIIYKNGDIVRFHRLKIQVYKKETQGITSSGFASLTFEGTLGAPIIPRTSS KYFNFTTEDHKMVEALRVWASTHMSPSWTLLKLCDVQPMQYFDLTCQLLGKAEVDGASFL LKVWDGTRTPFPSWRVLIQDLVLEGDLSHIHRLQNLTIDILVYDNHVHVARSLKVGSFLR IYSLHTKLQSMNSENQTMLSLEFHLHGGTSYGRGIRVLPESNSDVDQLKKDLESANLTAN QHSDVICQSEPDDSFPSSGSVSLYEVERCQQLSATILTDHQYLERTPLCAILKQKAPQQY RIRAKLRSYKPRRLFQSVKLHCPKCHLLQEVPHEGDLDIIFQDGATKTPDVKLQNTSLYD SKIWTTKNQKGRKVAVHFVKNNGILPLSNECLLLIEGGTLSEICKLSNKFNSVIPVRSGH EDLELLDLSAPFLIQGTIHHYGCKQCSSLRSIQNLNSLVDKTSWIPSSVAEALGIVPLQY VFVMTFTLDDGTGVLEAYLMDSDKFFQIPASEVLMDDDLQKSVDMIMDMFCPPGIKIDAY PWLECFIKSYNVTNGTDNQICYQIFDTTVAEDVI
Structural basis of human telomerase recruitment by TPP1-POT1. Sekne, Z., Ghanim, G.E., van Roon, A.M. et al. Science (2022) 375:1173-1176. DOI 10.1126/science.abn6840 · PubMed
Other PDB entries of the same protein (UniProt O14746 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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