9Q0Z: Telomerase reverse transcriptase

Human telomerase catalytic core with shelterin protein TPP1, BIBR1532 and DNA primer ending in AGGG. Determined by electron microscopy at 3.1 Å resolution. Released 17 Jun 2026.

Method
Electron microscopy
Resolution
3.1 Å
Organism
Homo sapiens
Chains
6
Atoms
14,706
Mol. weight
327.86 kDa
Ligands
55C
Released
17 Jun 2026

Explore 9Q0Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q0Z contains 72 α-helices and 53 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.

Chain A: 53 helices, 41 β-strands

ElementResiduesLengthSheet
α-helix8-1710
β-strand20-2341
α-helix24-318
α-helix45-539
β-strand54-5851
α-helix77-9115
β-strand101-10332
β-strand119-12132
α-helix126-1327
α-helix135-14410
α-helix146-15510
β-strand157-16261
β-strand166-17161
α-helix175-1773
β-strand325-32733
α-helix328-3314
β-strand33214
α-helix346-3494
α-helix354-36411
α-helix372-3743
α-helix379-3835
α-helix384-3874
α-helix390-40011
α-helix405-4128
α-helix445-4517
α-helix4551
β-strand45614
α-helix4571
α-helix458-47215
α-helix475-4784
α-helix481-49515
β-strand502-50433
α-helix505-5084
α-helix518-5203
α-helix531-54717
α-helix548-5536
α-helix554-5585
β-strand561-56554
β-strand573-57754
α-helix578-59619
β-strand598-60035
α-helix601-6022
α-helix603-6108
β-strand617-626105
β-strand629-63685
α-helix655-67117
α-helix673-6764
β-strand67916
α-helix683-69715
α-helix704-7063
β-strand707-71046
β-strand71217
β-strand71318
α-helix716-7194
α-helix722-73211
β-strand73819
β-strand740-751121
β-strand754-764111
α-helix773-78311
β-strand790-79781
β-strand80119
α-helix802-81413
β-strand816-82055
β-strand823-82755
β-strand833110
β-strand835110
α-helix838-85013
β-strand862-86546
β-strand86917
β-strand870-87456
α-helix877-88812
β-strand891111
α-helix892-8943
β-strand896111
β-strand89818
α-helix900-9023
β-strand904-90526
α-helix912-9143
β-strand92016
β-strand927-930412
β-strand933-936412
β-strand942-944312
α-helix946-9494
α-helix966-98116
α-helix984-9874
α-helix994-101623
α-helix1025-10273
α-helix1029-105022
β-strand1058113
β-strand1062113
α-helix1067-108115
α-helix1086-110621
α-helix1109-111810
α-helix1127-11293
Chain C: 10 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix99-1035
α-helix105-1073
β-strand113-1221016
α-helix125-1273
α-helix135-1373
β-strand143-147516
β-strand152-157616
α-helix159-1646
α-helix168-1714
α-helix173-1764
β-strand180-1921316
α-helix193-1942
β-strand195117
β-strand198117
α-helix199-2002
β-strand201-2151516
β-strand223116
α-helix228-23811
Chain F: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix39-4911
β-strand54-55214
α-helix57-8428
β-strand89-90215
α-helix92-10211
α-helix107-12317
Chain G: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix19-224
α-helix28-3710
β-strand43-44215
α-helix47-7327
β-strand78-79214
α-helix81-899
α-helix92-976

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Telomerase RNABRNA451Homo sapiens
Telomerase reverse transcriptaseAprotein1167Homo sapiensO14746 (AlphaFold model)
Telomeric repeat substrateDDNA18Homo sapiens
Histone H2B type 1-C/E/F/G/IFprotein126Homo sapiensP62807 (AlphaFold model)
Histone H2A.JGprotein129Homo sapiensQ9BTM1 (AlphaFold model)
Adrenocortical dysplasia protein homologCprotein163Homo sapiensQ96AP0 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>9Q0Z_1 Telomerase RNA (chains B)
GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG
AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG
GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC
AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA
ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG
AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC
AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG
GACGUGCACCCAGGACUCGGCUCACACAUGC
Sequence of entity 2 (A), FASTA
>9Q0Z_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
Sequence of entity 3 (D), FASTA
>9Q0Z_3 Telomeric repeat substrate (chains D)
TTAGGGTTAGGGTTAGGG
Sequence of entity 4 (F), FASTA
>9Q0Z_4 Histone H2B type 1-C/E/F/G/I (chains F)
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM
GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT
KYTSSK
Sequence of entity 5 (G), FASTA
>9Q0Z_5 Histone H2A.J (chains G)
MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK
TESQKTKSK
Sequence of entity 6 (C), FASTA
>9Q0Z_6 Adrenocortical dysplasia protein homolog (chains C)
GAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLV
SDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQV
DRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSN

Ligands and cofactors

IDNameFormulaCopies
55C2-{[(2E)-3-(naphthalen-2-yl)but-2-enoyl]amino}benzoic acidC21 H17 N O31

Primary citation

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:

Browse structure collections

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