The catalytic core lobe of human telomerase in complex with a telomeric DNA substrate. Determined by electron microscopy at 3.8 Å resolution. Released 28 Apr 2021.
Explore 7BG9 in 3D Show helices and sheets RCSB PDB PDBe
7BG9 contains 53 α-helices and 33 β-strands across 3 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 | 12-21 | 10 | |
| β-strand | 24-27 | 4 | 1 |
| α-helix | 32-35 | 4 | |
| α-helix | 48-51 | 4 | |
| β-strand | 55-58 | 4 | 1 |
| α-helix | 79-87 | 9 | |
| α-helix | 96-99 | 4 | |
| α-helix | 134-144 | 11 | |
| α-helix | 151-154 | 4 | |
| β-strand | 157-160 | 4 | 1 |
| β-strand | 168-169 | 2 | 1 |
| α-helix | 175-178 | 4 | |
| α-helix | 326-329 | 4 | |
| α-helix | 344-348 | 5 | |
| α-helix | 355-365 | 11 | |
| α-helix | 384-388 | 5 | |
| α-helix | 390-401 | 12 | |
| α-helix | 445-452 | 8 | |
| α-helix | 455 | 1 | |
| β-strand | 456 | 1 | 2 |
| α-helix | 457 | 1 | |
| α-helix | 458-469 | 12 | |
| α-helix | 475-478 | 4 | |
| α-helix | 481-495 | 15 | |
| α-helix | 531-557 | 27 | |
| β-strand | 561-564 | 4 | 2 |
| β-strand | 574-577 | 4 | 2 |
| α-helix | 578-594 | 17 | |
| α-helix | 598 | 1 | |
| β-strand | 599-600 | 2 | 3 |
| α-helix | 605-609 | 5 | |
| β-strand | 617 | 1 | 4 |
| β-strand | 619-625 | 7 | 5 |
| β-strand | 630-636 | 7 | 5 |
| α-helix | 654-671 | 18 | |
| α-helix | 673-675 | 3 | |
| β-strand | 680 | 1 | 6 |
| α-helix | 684-696 | 13 | |
| β-strand | 707-711 | 5 | 6 |
| α-helix | 722-732 | 11 | |
| β-strand | 739 | 1 | 7 |
| β-strand | 740-746 | 7 | 8 |
| β-strand | 755-761 | 7 | 8 |
| α-helix | 773-780 | 8 | |
| α-helix | 781-783 | 3 | |
| β-strand | 790-792 | 3 | 8 |
| α-helix | 799 | 1 | |
| β-strand | 800 | 1 | 7 |
| α-helix | 801 | 1 | |
| α-helix | 802-814 | 13 | |
| β-strand | 816 | 1 | 4 |
| β-strand | 818-820 | 3 | 3 |
| β-strand | 823-826 | 4 | 3 |
| α-helix | 838-853 | 16 | |
| β-strand | 862-866 | 5 | 6 |
| β-strand | 869-874 | 6 | 6 |
| α-helix | 877-888 | 12 | |
| β-strand | 904-906 | 3 | 6 |
| β-strand | 928-930 | 3 | 9 |
| β-strand | 933-935 | 3 | 9 |
| β-strand | 942-944 | 3 | 9 |
| α-helix | 954-957 | 4 | |
| α-helix | 966-981 | 16 | |
| α-helix | 984-987 | 4 | |
| α-helix | 995-1016 | 22 | |
| α-helix | 1025-1027 | 3 | |
| α-helix | 1029-1051 | 23 | |
| β-strand | 1058 | 1 | 10 |
| β-strand | 1062 | 1 | 10 |
| α-helix | 1067-1082 | 16 | |
| α-helix | 1086-1089 | 4 | |
| α-helix | 1095-1105 | 11 | |
| α-helix | 1110-1118 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| α-helix | 28-34 | 7 | |
| β-strand | 43-44 | 2 | 12 |
| α-helix | 47-73 | 27 | |
| β-strand | 79 | 1 | 11 |
| α-helix | 82-90 | 9 | |
| α-helix | 93-97 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-49 | 11 | |
| β-strand | 55 | 1 | 11 |
| α-helix | 57-85 | 29 | |
| β-strand | 89-90 | 2 | 12 |
| α-helix | 92-102 | 11 | |
| α-helix | 106-123 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomerase reverse transcriptase,Telomerase reverse transcriptase | A | protein | 1332 | Homo sapiens | O14746 (AlphaFold model) |
| DNA (5'-d(p*tp*tp*ap*gp*gp*g)-3') | N | DNA | 18 | synthetic construct | |
| Histone H2B | M | protein | 166 | Homo sapiens | B4DR52 (AlphaFold model) |
| Histone H2A | L | protein | 130 | Homo sapiens | P0C0S8 (AlphaFold model) |
| RNA (256-mer) | B | RNA | 451 | Homo sapiens |
>7BG9_1 Telomerase reverse transcriptase,Telomerase reverse transcriptase (chains A) MKTAALAQHDEAVDNKFNKEQQNAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEA KKLNDAQAPKVDNKFNKEQQNAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKK LNGAQAPKVDANSAGKSTDYDIPTTASENLYFQGHKLGTFQGPWSHPQFEKGSAGSAAGS GAGWSHPQFEKSRPTTASGTMPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQ RGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFG FALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFV LVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPG ARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAE EATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQ LRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNH AQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQ VYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWL RRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSV WSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVV GARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQ DPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFK SHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRI RGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHA KTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTL EVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTN IYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKG AAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAAN PALPSDFKTILD
>7BG9_2 DNA (5'-D(P*TP*TP*AP*GP*GP*G)-3') (chains N) TTTTTTTTTTTTTTAGGG
>7BG9_3 Histone H2B (chains M) MPDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT KYTSSNPRNLSPTKPGGSEDRQPPPSQLSAIPPFCLVLRAGIAGQV
>7BG9_4 Histone H2A (chains L) MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVRRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK TESHHKAKGK
>7BG9_5 RNA (256-MER) (chains B) GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG GACGUGCACCCAGGACUCGGCUCACACAUGC
Structure of human telomerase holoenzyme with bound telomeric DNA. Ghanim, G.E., Fountain, A.J., van Roon, A.M. et al. Nature (2021) 593:449-453. DOI 10.1038/s41586-021-03415-4 · 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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