Complex structure of viral RNA polymerase I. Determined by X-ray diffraction at 3.2 Å resolution. Released 8 Aug 2012.
Explore 3VNU in 3D Show helices and sheets RCSB PDB PDBe
3VNU contains 54 α-helices and 63 β-strands across 1 chain. 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 | 7-9 | 3 | |
| α-helix | 21-24 | 4 | |
| α-helix | 35-43 | 9 | |
| α-helix | 46-51 | 6 | |
| β-strand | 64-66 | 3 | 1 |
| β-strand | 70-77 | 8 | 1 |
| α-helix | 81-84 | 4 | |
| α-helix | 89-93 | 5 | |
| α-helix | 99-102 | 4 | |
| α-helix | 108-114 | 7 | |
| α-helix | 116-123 | 8 | |
| β-strand | 131-139 | 9 | 1 |
| β-strand | 142-144 | 3 | 2 |
| β-strand | 147-148 | 2 | 2 |
| β-strand | 152-158 | 7 | 2 |
| α-helix | 166-176 | 11 | |
| α-helix | 188-205 | 18 | |
| α-helix | 209-227 | 19 | |
| β-strand | 233 | 1 | 3 |
| β-strand | 241 | 1 | 3 |
| α-helix | 242-248 | 7 | |
| β-strand | 255-260 | 6 | 2 |
| α-helix | 272-284 | 13 | |
| β-strand | 296-303 | 8 | 4 |
| α-helix | 305-307 | 3 | |
| α-helix | 309-322 | 14 | |
| β-strand | 351-352 | 2 | 4 |
| β-strand | 355 | 1 | 4 |
| β-strand | 360-365 | 6 | 4 |
| α-helix | 370-376 | 7 | |
| β-strand | 385-391 | 7 | 4 |
| α-helix | 400-408 | 9 | |
| β-strand | 416-420 | 5 | 4 |
| α-helix | 428-443 | 16 | |
| α-helix | 449-451 | 3 | |
| β-strand | 454-456 | 3 | 4 |
| α-helix | 459-463 | 5 | |
| α-helix | 467-477 | 11 | |
| α-helix | 485-487 | 3 | |
| β-strand | 496-498 | 3 | 5 |
| β-strand | 501-505 | 5 | 6 |
| β-strand | 509-516 | 8 | 6 |
| β-strand | 518 | 1 | 5 |
| β-strand | 521-522 | 2 | 7 |
| β-strand | 526-530 | 5 | 5 |
| β-strand | 536-539 | 4 | 5 |
| β-strand | 540-544 | 5 | 6 |
| β-strand | 552-553 | 2 | 7 |
| β-strand | 557-563 | 7 | 6 |
| α-helix | 568-570 | 3 | |
| β-strand | 573 | 1 | 8 |
| β-strand | 575 | 1 | 8 |
| β-strand | 576-578 | 3 | 5 |
| β-strand | 584-595 | 12 | 9 |
| α-helix | 596 | 1 | |
| α-helix | 598-600 | 3 | |
| β-strand | 607 | 1 | 10 |
| β-strand | 614 | 1 | 9 |
| β-strand | 623-625 | 3 | 9 |
| β-strand | 635 | 1 | 10 |
| β-strand | 640-653 | 14 | 9 |
| β-strand | 658-663 | 6 | 9 |
| β-strand | 666-676 | 11 | 9 |
| α-helix | 703-713 | 11 | |
| α-helix | 723-732 | 10 | |
| α-helix | 733-735 | 3 | |
| α-helix | 737-740 | 4 | |
| α-helix | 745-747 | 3 | |
| α-helix | 757-769 | 13 | |
| α-helix | 784-803 | 20 | |
| α-helix | 817-833 | 17 | |
| α-helix | 840-843 | 4 | |
| α-helix | 864-867 | 4 | |
| β-strand | 873 | 1 | 11 |
| α-helix | 875-877 | 3 | |
| α-helix | 878-885 | 8 | |
| β-strand | 897 | 1 | 11 |
| β-strand | 902-903 | 2 | 12 |
| β-strand | 907 | 1 | 13 |
| β-strand | 913 | 1 | 13 |
| β-strand | 917-918 | 2 | 12 |
| α-helix | 921-936 | 16 | |
| α-helix | 937-939 | 3 | |
| α-helix | 949-961 | 13 | |
| β-strand | 964-967 | 4 | 14 |
| β-strand | 969 | 1 | 15 |
| α-helix | 972-975 | 4 | |
| β-strand | 977 | 1 | 16 |
| α-helix | 978-984 | 7 | |
| α-helix | 987-995 | 9 | |
| β-strand | 1000-1002 | 3 | 12 |
| β-strand | 1008-1010 | 3 | 12 |
| β-strand | 1013 | 1 | 16 |
| α-helix | 1022-1039 | 18 | |
| α-helix | 1045-1047 | 3 | |
| β-strand | 1049-1051 | 3 | 14 |
| β-strand | 1054-1058 | 5 | 14 |
| α-helix | 1059-1061 | 3 | |
| α-helix | 1062-1071 | 10 | |
| β-strand | 1076 | 1 | 15 |
| β-strand | 1082 | 1 | 14 |
| β-strand | 1087-1090 | 4 | 17 |
| β-strand | 1093-1096 | 4 | 17 |
| β-strand | 1099-1100 | 2 | 17 |
| α-helix | 1109-1110 | 2 | |
| α-helix | 1113-1126 | 14 | |
| β-strand | 1128-1129 | 2 | 18 |
| β-strand | 1132-1133 | 2 | 18 |
| α-helix | 1135-1145 | 11 | |
| α-helix | 1151-1154 | 4 | |
| β-strand | 1156-1157 | 2 | 19 |
| β-strand | 1166-1167 | 2 | 19 |
| β-strand | 1177-1179 | 3 | 20 |
| β-strand | 1182-1195 | 14 | 20 |
| α-helix | 1199-1212 | 14 | |
| α-helix | 1242-1245 | 4 | |
| β-strand | 1247-1260 | 14 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicase | A | protein | 1289 | Escherichia coli O157:H7, Escherichia phage Qbeta | P0A6N3 (AlphaFold model), P0A6P3 (AlphaFold model), P14647 |
| RNA (5'-r(*cp*cp*cp*up*ap*cp*cp*c)-3') | G | RNA | 8 | ||
| RNA (5'-r(*gp*gp*gp*up*ap*gp*gp*g)-3') | T | RNA | 8 |
>3VNU_1 Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicase (chains A) MAEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADG VIKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERV ALVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEF IKPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSK TVGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQSHMSKEKFERTKPHVNVG TIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRH YAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLN KCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFL DSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTC TGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDE GGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFA IREGGRTVGAGVVAKVLSGASGAAGGGGSGGGGSMSKTASSRNSLSAQLRRAANTRIEVE GNLALSIANDLLLAYGQSPFNSEAECISFSPRFDGTPDDFRINYLKAEIMSKYDDFSLGI DTEAVAWEKFLAAEAECALTNARLYRPDYSEDFNFSLGESCIHMARRKIAKLIGDVPSVE GMLRHCRFSGGATTTNNRSYGHPSFKFALPQACTPRALKYVLALRASTHFDIRISDISPF NKAVTVPKNSKTDRCIAIEPGWNMFFQLGIGGILRDRLRCWGIDLNDQTINQRRAHEGSV TNNLATVDLSAASDSISLALCELLLPPGWFEVLMDLRSPKGRLPDGSVVTYEKISSMGNG YTFELESLIFASLARSVCEILDLDSSEVTVYGDDIILPSCAVPALREVFKYVGFTTNTKK TFSEGPFRESCGKHYYSGVDVTPFYIRHRIVSPADLILVLNNLYRWATIDGVWDPRAHSV YLKYRKLLPKQLQRNTIPDGYGDGALVGSVLINPFAKNRGWIRYVPVITDHTRDRERAEL GSYLYDLFSRCLSESNDGLPLRGPSGCDSADLFAIDQLICRSNPTKISRSTGKFDIQYIA CSSRVLAPYGVFQGTKVASLHEAHHHHHH
>3VNU_2 RNA (5'-R(*CP*CP*CP*UP*AP*CP*CP*C)-3') (chains G) CCCUACCC
>3VNU_3 RNA (5'-R(*GP*GP*GP*UP*AP*GP*GP*G)-3') (chains T) GGGUAGGG
Mechanism for template-independent terminal adenylation activity of Q beta replicase. Takeshita, D., Yamashita, S., Tomita, K. Structure (2012) 20:1661-1669. DOI 10.1016/j.str.2012.07.004 · PubMed
Other PDB entries of the same protein (UniProt P0A6N3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3VNU 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.