Human telomerase catalytic core with shelterin protein TPP1, dTpNHpp and DNA primer ending in AGGG. Determined by electron microscopy at 2.9 Å resolution. Released 17 Jun 2026.
Explore 9Q10 in 3D Show helices and sheets RCSB PDB PDBe
9Q10 contains 64 α-helices and 49 β-strands across 4 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 | 8-15 | 8 | |
| β-strand | 22-23 | 2 | 1 |
| α-helix | 24-31 | 8 | |
| α-helix | 45-53 | 9 | |
| β-strand | 54-57 | 4 | 1 |
| α-helix | 63-66 | 4 | |
| α-helix | 77-91 | 15 | |
| β-strand | 101-103 | 3 | 2 |
| β-strand | 119-121 | 3 | 2 |
| α-helix | 126-132 | 7 | |
| α-helix | 136-144 | 9 | |
| α-helix | 146-155 | 10 | |
| β-strand | 157-161 | 5 | 1 |
| β-strand | 167-169 | 3 | 1 |
| β-strand | 325-327 | 3 | 3 |
| β-strand | 332 | 1 | 4 |
| α-helix | 346-349 | 4 | |
| α-helix | 356-364 | 9 | |
| α-helix | 372-374 | 3 | |
| α-helix | 379-383 | 5 | |
| α-helix | 384-387 | 4 | |
| α-helix | 390-402 | 13 | |
| α-helix | 405-412 | 8 | |
| α-helix | 444-451 | 8 | |
| β-strand | 455-456 | 2 | 4 |
| α-helix | 457 | 1 | |
| α-helix | 460-472 | 13 | |
| 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 | 531-547 | 17 | |
| α-helix | 548-552 | 5 | |
| α-helix | 553-560 | 8 | |
| β-strand | 561-565 | 5 | 4 |
| β-strand | 573-577 | 5 | 4 |
| α-helix | 578-595 | 18 | |
| β-strand | 598-600 | 3 | 5 |
| α-helix | 601-602 | 2 | |
| α-helix | 603-610 | 8 | |
| β-strand | 618-626 | 9 | 5 |
| β-strand | 629-636 | 8 | 5 |
| α-helix | 652-671 | 20 | |
| α-helix | 673-676 | 4 | |
| β-strand | 679 | 1 | 6 |
| α-helix | 683-697 | 15 | |
| β-strand | 707-712 | 6 | 6 |
| β-strand | 713 | 1 | 7 |
| α-helix | 716-719 | 4 | |
| α-helix | 724-732 | 9 | |
| β-strand | 738-749 | 12 | 1 |
| β-strand | 755-764 | 10 | 1 |
| α-helix | 766-768 | 3 | |
| α-helix | 773-782 | 10 | |
| β-strand | 790-801 | 12 | 1 |
| α-helix | 802-814 | 13 | |
| β-strand | 817-820 | 4 | 5 |
| β-strand | 823-827 | 5 | 5 |
| α-helix | 838-846 | 9 | |
| β-strand | 862-865 | 4 | 6 |
| β-strand | 869-874 | 6 | 6 |
| α-helix | 877-888 | 12 | |
| β-strand | 891 | 1 | 8 |
| β-strand | 896 | 1 | 8 |
| β-strand | 898 | 1 | 7 |
| β-strand | 904-905 | 2 | 6 |
| α-helix | 912-914 | 3 | |
| β-strand | 920-921 | 2 | 6 |
| β-strand | 927-929 | 3 | 9 |
| β-strand | 933-936 | 4 | 9 |
| β-strand | 942-944 | 3 | 9 |
| β-strand | 953 | 1 | 10 |
| α-helix | 968-981 | 14 | |
| α-helix | 984-987 | 4 | |
| α-helix | 994-1016 | 23 | |
| α-helix | 1030-1050 | 21 | |
| β-strand | 1058 | 1 | 11 |
| β-strand | 1062 | 1 | 11 |
| α-helix | 1067-1082 | 16 | |
| α-helix | 1086-1097 | 12 | |
| α-helix | 1099-1106 | 8 | |
| α-helix | 1109-1118 | 10 | |
| β-strand | 1131 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 99-103 | 5 | |
| α-helix | 105-107 | 3 | |
| β-strand | 113-122 | 10 | 12 |
| α-helix | 125-127 | 3 | |
| α-helix | 135-137 | 3 | |
| β-strand | 143-147 | 5 | 12 |
| β-strand | 152-157 | 6 | 12 |
| α-helix | 159-164 | 6 | |
| α-helix | 168-172 | 5 | |
| β-strand | 180-192 | 13 | 12 |
| α-helix | 193 | 1 | |
| β-strand | 195 | 1 | 13 |
| β-strand | 198 | 1 | 13 |
| β-strand | 201-215 | 15 | 12 |
| β-strand | 223 | 1 | 12 |
| α-helix | 228-238 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| α-helix | 28-37 | 10 | |
| β-strand | 44 | 1 | 14 |
| α-helix | 47-72 | 26 | |
| β-strand | 78-79 | 2 | 15 |
| α-helix | 81-88 | 8 | |
| α-helix | 92-95 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-49 | 11 | |
| β-strand | 54-55 | 2 | 15 |
| α-helix | 57-84 | 28 | |
| β-strand | 90 | 1 | 14 |
| α-helix | 92-102 | 11 | |
| α-helix | 107-124 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomerase RNA | B | RNA | 451 | Homo sapiens | |
| Telomerase reverse transcriptase | A | protein | 1167 | Homo sapiens | O14746 (AlphaFold model) |
| Telomeric repeat substrate | D | DNA | 18 | Homo sapiens | |
| Adrenocortical dysplasia protein homolog | C | protein | 163 | Homo sapiens | Q96AP0 (AlphaFold model) |
| Histone H2A.J | F | protein | 129 | Homo sapiens | Q9BTM1 (AlphaFold model) |
| Histone H2B type 1-C/E/F/G/I | G | protein | 126 | Homo sapiens | P62807 (AlphaFold model) |
>9Q10_1 Telomerase RNA (chains B) GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG GACGUGCACCCAGGACUCGGCUCACACAUGC
>9Q10_2 Telomerase reverse transcriptase (chains A) GHMSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSAMPRAPRCRAVRSLLRSHYREVLPLA TFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVL QRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVG DDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNH SVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGP SDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVY AETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQR YWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDP RRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSL QELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTE TTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIP KPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDD IHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYA VVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGL FDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLR LVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAH GLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSL FLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYS ILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSR KLPGTTLTALEAAANPALPSDFKTILD
>9Q10_3 Telomeric repeat substrate (chains D) TTAGGGTTAGGGTTAGGG
>9Q10_4 Adrenocortical dysplasia protein homolog (chains C) GAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLV SDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQV DRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSN
>9Q10_5 Histone H2A.J (chains F) MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK TESQKTKSK
>9Q10_6 Histone H2B type 1-C/E/F/G/I (chains G) MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT KYTSSK
| ID | Name | Formula | Copies |
|---|---|---|---|
| 1FZ | 5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]thymidi… | C10 H18 N3 O13 P3 | 1 |
Structures of human telomerase with BIBR1532 reveal novel mechanism of inhibition. Wang, Y., Liu, B., He, Y. et al. Nat Chem Biol (2026). DOI 10.1038/s41589-026-02238-6 · 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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