9Q14: Adrenocortical dysplasia protein homolog

Human telomerase catalytic core with shelterin protein TPP1, BIBR1532 and DNA primer ending in TTAG. Determined by electron microscopy at 3.0 Å resolution. Released 17 Jun 2026.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 6
Atoms: 14,741
Mol. weight: 327.86 kDa
Ligands: 55C
Released: 17 Jun 2026

Explore 9Q14 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q14 contains 74 α-helices and 48 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: 56 helices, 36 β-strands

Element	Residues	Length	Sheet
α-helix	8-17	10
β-strand	18-23	6	5
α-helix	24-31	8
α-helix	45-53	9
β-strand	54-59	6	5
β-strand	72	1	6
α-helix	77-91	15
α-helix	96-98	3
β-strand	101-103	3	7
β-strand	119-121	3	7
α-helix	126-132	7
α-helix	136-144	9
β-strand	145	1	6
α-helix	146-155	10
β-strand	157-162	6	5
β-strand	166-171	6	5
α-helix	175-177	3
β-strand	325-327	3	8
α-helix	328-331	4
α-helix	346-349	4
α-helix	354-361	8
α-helix	362-366	5
α-helix	372-374	3
α-helix	384-387	4
α-helix	390-400	11
α-helix	405-412	8
α-helix	444-451	8
α-helix	455	1
β-strand	456	1	9
α-helix	457	1
α-helix	458-472	15
α-helix	475-478	4
α-helix	481-495	15
β-strand	502-504	3	8
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	9
β-strand	574-577	4	9
α-helix	578-592	15
β-strand	598-600	3	10
α-helix	601-602	2
α-helix	603-611	9
α-helix	615-616	2
β-strand	617-626	10	10
β-strand	629-636	8	10
α-helix	641-643	3
α-helix	648-671	24
α-helix	673-675	3
β-strand	679	1	11
α-helix	683-697	15
β-strand	707-712	6	11
β-strand	713	1	12
α-helix	716-719	4
α-helix	722-732	11
β-strand	738-750	13	5
α-helix	751-753	3
β-strand	754-764	11	5
α-helix	773-783	11
β-strand	789-801	13	5
α-helix	802-814	13
β-strand	816-820	5	10
β-strand	823-827	5	10
α-helix	838-852	15
α-helix	857-859	3
β-strand	862-865	4	11
β-strand	869-874	6	11
α-helix	877-887	11
β-strand	891	1	13
α-helix	892-894	3
β-strand	896	1	13
β-strand	898	1	12
β-strand	903-905	3	11
α-helix	912-914	3
β-strand	919-921	3	11
β-strand	927-930	4	14
β-strand	933-936	4	14
β-strand	942-944	3	14
β-strand	953	1	15
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
α-helix	1059-1061	3
α-helix	1067-1082	16
α-helix	1086-1106	21
α-helix	1109-1118	10
α-helix	1127-1129	3
β-strand	1131	1	15

Chain C: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	101-104	4
β-strand	113-122	10	1
α-helix	125-127	3
α-helix	135-137	3
β-strand	143-147	5	1
β-strand	152-157	6	1
α-helix	159-163	5
α-helix	168-172	5
β-strand	180-192	13	1
β-strand	195	1	2
β-strand	198	1	2
α-helix	199-200	2
β-strand	201-215	15	1
α-helix	221-222	2
β-strand	223	1	1
α-helix	224-226	3
α-helix	228-239	12

Chain F: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	19-21	3
α-helix	28-37	10
β-strand	43-44	2	3
α-helix	47-73	27
β-strand	78-79	2	4
α-helix	81-90	10
α-helix	92-97	6

Chain G: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	39-47	9
β-strand	54-55	2	4
α-helix	57-84	28
β-strand	89-90	2	3
α-helix	92-102	11
α-helix	107-124	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
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)
Telomeric repeat substrate	D	DNA	18	Homo sapiens
Telomerase RNA	B	RNA	451	Homo sapiens
Telomerase reverse transcriptase	A	protein	1167	Homo sapiens	O14746 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>9Q14_1 Adrenocortical dysplasia protein homolog (chains C)
GAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLV
SDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQV
DRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSN

Sequence of entity 2 (F), FASTA

>9Q14_2 Histone H2A.J (chains F)
MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK
TESQKTKSK

Sequence of entity 3 (G), FASTA

>9Q14_3 Histone H2B type 1-C/E/F/G/I (chains G)
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM
GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT
KYTSSK

Sequence of entity 4 (D), FASTA

>9Q14_4 Telomeric repeat substrate (chains D)
GGTTAGGGTTAGGGTTAG

Sequence of entity 5 (B), FASTA

>9Q14_5 Telomerase RNA (chains B)
GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG
AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG
GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC
AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA
ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG
AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC
AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG
GACGUGCACCCAGGACUCGGCUCACACAUGC

Sequence of entity 6 (A), FASTA

>9Q14_6 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

Ligands and cofactors

ID	Name	Formula	Copies
55C	2-{[(2E)-3-(naphthalen-2-yl)but-2-enoyl]amino}benzoic acid	C21 H17 N O3	1

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 Q96AP0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5H65 2.1 Å, Crystal structure of human POT1 and TPP1
5UN7 2.1 Å, Structure of the human POT1-TPP1 telomeric complex
5XYF 2.2 Å, Crystal structure of the human TIN2-TPP1-TRF2 telomeric complex
2I46 2.7 Å, Crystal structure of human TPP1
9Q16 2.7 Å, Human telomerase catalytic core with shelterin protein TPP1, dGpNHpp and DNA primer…
9Q12 2.8 Å, Human telomerase catalytic core with shelterin protein TPP1 and DNA primer ending in TTAG
7S1T 2.9 Å, Structure of the human POT1-TPP1 complex
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…
5I2X 3.0 Å, Crystal Structure of TPP1 K170del
5I2Y 3.0 Å, Crystal Structure of TPP1 K170A
9Q0Z 3.1 Å, Human telomerase catalytic core with shelterin protein TPP1, BIBR1532 and DNA primer…

Browse structure collections

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