9Q12: Telomerase reverse transcriptase

Human telomerase catalytic core with shelterin protein TPP1 and DNA primer ending in TTAG. Determined by electron microscopy at 2.8 Å resolution. Released 17 Jun 2026.

Method: Electron microscopy
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 6
Atoms: 14,571
Mol. weight: 328.78 kDa
Released: 17 Jun 2026

Explore 9Q12 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q12 contains 72 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.

Chain A: 54 helices, 37 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
β-strand	20-23	4	1
α-helix	24-31	8
α-helix	45-53	9
β-strand	54-58	5	1
α-helix	77-91	15
α-helix	96-98	3
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	157-162	6	1
β-strand	166-171	6	1
α-helix	175-177	3
β-strand	325-327	3	3
α-helix	328-331	4
β-strand	332	1	4
α-helix	346-349	4
α-helix	356-365	10
α-helix	379-383	5
α-helix	384-387	4
α-helix	390-400	11
α-helix	405-412	8
α-helix	445-452	8
α-helix	455	1
β-strand	456	1	4
α-helix	457	1
α-helix	458-472	15
α-helix	475-478	4
α-helix	481-495	15
β-strand	502-504	3	3
α-helix	505-509	5
α-helix	518-520	3
α-helix	531-547	17
α-helix	548-553	6
α-helix	554-560	7
β-strand	561-564	4	4
β-strand	574-577	4	4
α-helix	578-595	18
β-strand	598-600	3	5
α-helix	601-602	2
α-helix	603-611	9
α-helix	615-617	3
β-strand	618-626	9	5
β-strand	629-636	8	5
α-helix	653-671	19
α-helix	673-675	3
β-strand	679	1	6
α-helix	683-697	15
β-strand	707-711	5	6
β-strand	713	1	7
α-helix	716-719	4
α-helix	722-730	9
β-strand	738-748	11	1
β-strand	756-764	9	1
α-helix	766-768	3
α-helix	773-781	9
β-strand	789-801	13	1
α-helix	802-814	13
β-strand	817-820	4	5
β-strand	823-827	5	5
α-helix	838-853	16
β-strand	862-865	4	6
β-strand	870-874	5	6
α-helix	877-889	13
β-strand	891	1	8
α-helix	892-894	3
β-strand	896	1	8
β-strand	898	1	7
α-helix	900-902	3
β-strand	904-905	2	6
α-helix	912-914	3
β-strand	920-921	2	6
α-helix	922-923	2
β-strand	927-930	4	9
β-strand	933-936	4	9
β-strand	942-944	3	9
α-helix	947-949	3
β-strand	953	1	10
α-helix	966-981	16
α-helix	984-987	4
α-helix	994-1016	23
α-helix	1025-1027	3
α-helix	1029-1050	22
β-strand	1058	1	11
β-strand	1062	1	11
α-helix	1067-1083	17
α-helix	1086-1106	21
α-helix	1109-1118	10
β-strand	1131	1	10

Chain C: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	99-103	5
α-helix	105-107	3
β-strand	113-122	10	14
α-helix	135-137	3
β-strand	143-147	5	14
β-strand	152-157	6	14
α-helix	159-164	6
α-helix	168-172	5
α-helix	174-176	3
β-strand	180-192	13	14
α-helix	193	1
β-strand	195	1	15
β-strand	198	1	15
α-helix	199-200	2
β-strand	201-215	15	14
β-strand	223	1	14
α-helix	228-238	11

Chain F: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	19-22	4
α-helix	28-37	10
β-strand	43-44	2	12
α-helix	47-73	27
β-strand	78-79	2	13
α-helix	81-90	10
α-helix	92-98	7

Chain G: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	39-49	11
β-strand	54-55	2	13
α-helix	57-84	28
β-strand	89-90	2	12
α-helix	92-102	11
α-helix	107-124	18

Molecules and chains

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	22	Homo sapiens
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)
Adrenocortical dysplasia protein homolog	C	protein	163	Homo sapiens	Q96AP0 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>9Q12_1 Telomerase RNA (chains B)
GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG
AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG
GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC
AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA
ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG
AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC
AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG
GACGUGCACCCAGGACUCGGCUCACACAUGC

Sequence of entity 2 (A), FASTA

>9Q12_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

>9Q12_3 Telomeric repeat substrate (chains D)
TTAGGGTTAGGGTTAGGGTTAG

Sequence of entity 4 (F), FASTA

>9Q12_4 Histone H2A.J (chains F)
MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK
TESQKTKSK

Sequence of entity 5 (G), FASTA

>9Q12_5 Histone H2B type 1-C/E/F/G/I (chains G)
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM
GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT
KYTSSK

Sequence of entity 6 (C), FASTA

>9Q12_6 Adrenocortical dysplasia protein homolog (chains C)
GAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLV
SDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQV
DRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSN

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:

5MEO 1.77 Å, Human Leukocyte Antigen presenting ILGKFLHRL
5MER 1.88 Å, Human Leukocyte Antigen A02 presenting ILAKFLHEL
5MEQ 2.27 Å, Human Leukocyte Antigen A02 presenting ILAKFLHTL
5UGW 2.31 Å, Structure of the human telomerase thumb domain
4B18 2.52 Å, The crystal structure of human Importin alpha 5 with TERT NLS peptide
9Q16 2.7 Å, Human telomerase catalytic core with shelterin protein TPP1, dGpNHpp and DNA primer…
5MEP 2.71 Å, Human Leukocyte Antigen A02 presenting ILGKFLHWL
4MNQ 2.74 Å, TCR-peptide specificity overrides affinity enhancing TCR-MHC interactions
2BCK 2.8 Å, Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide
5MEN 2.81 Å, Human Leukocyte Antigen A02 presenting ILAKFLHWL, in complex with cognate T-Cell Receptor
9Q10 2.9 Å, Human telomerase catalytic core with shelterin protein TPP1, dTpNHpp and DNA primer…
9Q11 2.9 Å, Human telomerase catalytic core with shelterin protein TPP1, BIBR1532, dTpNHpp and DNA…

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