catalytic core of human telomerase holoenzyme. Determined by electron microscopy at 3.54 Å resolution. Released 30 Mar 2022.
Explore 7V99 in 3D Show helices and sheets RCSB PDB PDBe
7V99 contains 50 α-helices and 34 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 | 5-17 | 13 | |
| β-strand | 21-23 | 3 | 1 |
| α-helix | 24-28 | 5 | |
| α-helix | 32-41 | 10 | |
| α-helix | 45-52 | 8 | |
| β-strand | 54-57 | 4 | 1 |
| α-helix | 77-91 | 15 | |
| β-strand | 95 | 1 | 2 |
| β-strand | 102-103 | 2 | 3 |
| β-strand | 106-108 | 3 | 4 |
| β-strand | 113-115 | 3 | 4 |
| β-strand | 118-119 | 2 | 3 |
| α-helix | 123-130 | 8 | |
| α-helix | 133-139 | 7 | |
| α-helix | 144-153 | 10 | |
| β-strand | 157-162 | 6 | 1 |
| β-strand | 168-170 | 3 | 1 |
| β-strand | 174 | 1 | 2 |
| α-helix | 176-179 | 4 | |
| α-helix | 323-324 | 2 | |
| β-strand | 325-326 | 2 | 5 |
| α-helix | 346-349 | 4 | |
| α-helix | 354-358 | 5 | |
| α-helix | 385-388 | 4 | |
| α-helix | 391-401 | 11 | |
| α-helix | 405-412 | 8 | |
| α-helix | 416-429 | 14 | |
| α-helix | 437-453 | 17 | |
| α-helix | 458-470 | 13 | |
| α-helix | 475-478 | 4 | |
| α-helix | 481-495 | 15 | |
| α-helix | 502 | 1 | |
| β-strand | 503-504 | 2 | 5 |
| α-helix | 505-508 | 4 | |
| α-helix | 531-557 | 27 | |
| β-strand | 561-564 | 4 | 6 |
| β-strand | 574-577 | 4 | 6 |
| α-helix | 578-595 | 18 | |
| β-strand | 598-600 | 3 | 7 |
| α-helix | 603-610 | 8 | |
| β-strand | 617-625 | 9 | 7 |
| β-strand | 630-637 | 8 | 7 |
| α-helix | 645-671 | 27 | |
| α-helix | 683-698 | 16 | |
| α-helix | 703-705 | 3 | |
| β-strand | 707-713 | 7 | 8 |
| α-helix | 722-736 | 15 | |
| β-strand | 740-750 | 11 | 1 |
| β-strand | 755-765 | 11 | 1 |
| α-helix | 773-782 | 10 | |
| β-strand | 789-799 | 11 | 1 |
| α-helix | 802-814 | 13 | |
| β-strand | 816-819 | 4 | 7 |
| β-strand | 824-827 | 4 | 7 |
| α-helix | 836-853 | 18 | |
| α-helix | 857-860 | 4 | |
| β-strand | 862-865 | 4 | 8 |
| β-strand | 870-874 | 5 | 8 |
| α-helix | 877-888 | 12 | |
| β-strand | 900-906 | 7 | 8 |
| β-strand | 920 | 1 | 8 |
| β-strand | 928-929 | 2 | 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 | 994-1017 | 24 | |
| α-helix | 1030-1050 | 21 | |
| α-helix | 1067-1082 | 16 | |
| α-helix | 1091-1106 | 16 | |
| α-helix | 1109-1118 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-21 | 5 | |
| α-helix | 28-36 | 9 | |
| β-strand | 42-43 | 2 | 10 |
| α-helix | 47-71 | 25 | |
| β-strand | 77-78 | 2 | 11 |
| α-helix | 80-89 | 10 | |
| α-helix | 91-97 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 38-48 | 11 | |
| β-strand | 53-54 | 2 | 11 |
| α-helix | 56-82 | 27 | |
| β-strand | 88-89 | 2 | 10 |
| α-helix | 91-101 | 11 | |
| α-helix | 104-123 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomerase reverse transcriptase | A | protein | 1132 | Homo sapiens | O14746 (AlphaFold model) |
| Histone H2A type 1-B/E | K | protein | 129 | Homo sapiens | P04908 (AlphaFold model) |
| Histone H2B type 1-K | L | protein | 125 | Homo sapiens | O60814 (AlphaFold model) |
| Telomerase RNA component | R | RNA | 451 | Homo sapiens | |
| Primer DNA | S | DNA | 24 | Homo sapiens |
>7V99_1 Telomerase reverse transcriptase (chains A) MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPW DARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVR SYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGA ATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRR GAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVG RQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRL VETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVT PAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGS RHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEI LAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRE LSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKA LFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTI PQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHL QETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTL LCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNL RKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTF NRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLP FHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLL KLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD
>7V99_2 Histone H2A type 1-B/E (chains K) SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTA EILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKT ESHHKAKGK
>7V99_3 Histone H2B type 1-K (chains L) PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMG IMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTK YTSAK
>7V99_4 Telomerase RNA component (chains R) GGGUUGCGGAGGGUGGGCCUGGGAGGGGUGGUGGCCAUUUUUUGUCUAACCCUAACUGAG AAGGGCGUAGGCGCCGUGCUUUUGCUCCCCGCGCGCUGUUUUUCUCGCUGACUUUCAGCG GGCGGAAAAGCCUCGGCCUGCCGCCUUCCACCGUUCAUUCUAGAGCAAACAAAAAAUGUC AGCUGCUGGCCCGUUCGCCCCUCCCGGGGACCUGCGGCGGGUCGCCUGCCCAGCCCCCGA ACCCCGCCUGGAGGCCGCGGUCGGCCCGGGGCUUCUCCGGAGGCACCCACUGCCACCGCG AAGAGUUGGGCUCUGUCAGCCGCGGGUCUCUCGGGGGCGAGGGCGAGGUUCAGGCCUUUC AGGCCGCAGGAAGAGGAACGGAGCGAGUCCCCGCGCGCGGCGCGAUUCCCUGAGCUGUGG GACGUGCACCCAGGACUCGGCUCACACAUGC
>7V99_5 Primer DNA (chains S) TTTTTTTTTTTTTTTTTTTTAGGG
Zipper head mechanism of telomere synthesis by human telomerase. Wan, F., Ding, Y., Zhang, Y. et al. Cell Res (2021) 31:1275-1290. DOI 10.1038/s41422-021-00586-7 · PubMed
Other PDB entries of the same protein (UniProt O14746 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7V99 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.