Structure of viral RNA polymerase complex 2. Determined by X-ray diffraction at 2.91 Å resolution. Released 18 Jan 2012.
Explore 3AVU in 3D Show helices and sheets RCSB PDB PDBe
3AVU contains 52 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 | 10-14 | 5 | |
| α-helix | 20-24 | 5 | |
| α-helix | 34-42 | 9 | |
| α-helix | 46-49 | 4 | |
| α-helix | 50-52 | 3 | |
| β-strand | 59-67 | 9 | 1 |
| β-strand | 70-78 | 9 | 1 |
| α-helix | 81-84 | 4 | |
| α-helix | 88-101 | 14 | |
| α-helix | 111-114 | 4 | |
| α-helix | 116-126 | 11 | |
| β-strand | 131-139 | 9 | 1 |
| β-strand | 143-144 | 2 | 2 |
| β-strand | 147-148 | 2 | 2 |
| β-strand | 152-157 | 6 | 2 |
| α-helix | 163-176 | 14 | |
| β-strand | 180 | 1 | 3 |
| α-helix | 190-204 | 15 | |
| α-helix | 209-227 | 19 | |
| β-strand | 228 | 1 | 3 |
| α-helix | 229-231 | 3 | |
| β-strand | 233-234 | 2 | 4 |
| β-strand | 237-241 | 5 | 4 |
| α-helix | 242-249 | 8 | |
| β-strand | 255-260 | 6 | 2 |
| α-helix | 273-284 | 12 | |
| β-strand | 296-303 | 8 | 5 |
| α-helix | 309-318 | 10 | |
| β-strand | 352-355 | 4 | 5 |
| β-strand | 360-365 | 6 | 5 |
| α-helix | 369-377 | 9 | |
| β-strand | 385-391 | 7 | 5 |
| α-helix | 400-410 | 11 | |
| β-strand | 415-420 | 6 | 5 |
| α-helix | 428-430 | 3 | |
| α-helix | 431-443 | 13 | |
| β-strand | 454-456 | 3 | 5 |
| α-helix | 459-463 | 5 | |
| α-helix | 467-480 | 14 | |
| α-helix | 485-486 | 2 | |
| α-helix | 490-492 | 3 | |
| α-helix | 494-495 | 2 | |
| β-strand | 496 | 1 | 6 |
| β-strand | 501-504 | 4 | 7 |
| β-strand | 510-515 | 6 | 7 |
| β-strand | 518 | 1 | 6 |
| β-strand | 520-522 | 3 | 8 |
| β-strand | 526-529 | 4 | 6 |
| β-strand | 536-539 | 4 | 6 |
| β-strand | 542-544 | 3 | 7 |
| β-strand | 549-550 | 2 | 7 |
| β-strand | 552-554 | 3 | 8 |
| β-strand | 558-563 | 6 | 7 |
| β-strand | 578 | 1 | 6 |
| β-strand | 585-595 | 11 | 9 |
| α-helix | 598-600 | 3 | |
| β-strand | 607 | 1 | 10 |
| β-strand | 614-616 | 3 | 9 |
| β-strand | 623-627 | 5 | 9 |
| β-strand | 635 | 1 | 10 |
| β-strand | 640-652 | 13 | 9 |
| β-strand | 658-663 | 6 | 9 |
| β-strand | 666-675 | 10 | 9 |
| α-helix | 703-713 | 11 | |
| α-helix | 723-735 | 13 | |
| α-helix | 738-740 | 3 | |
| α-helix | 743-746 | 4 | |
| α-helix | 757-768 | 12 | |
| α-helix | 784-803 | 20 | |
| α-helix | 817-833 | 17 | |
| α-helix | 839-844 | 6 | |
| α-helix | 858-860 | 3 | |
| α-helix | 863-868 | 6 | |
| β-strand | 871 | 1 | 11 |
| α-helix | 875-877 | 3 | |
| α-helix | 878-885 | 8 | |
| β-strand | 894 | 1 | 11 |
| β-strand | 900-906 | 7 | 12 |
| β-strand | 914-918 | 5 | 12 |
| α-helix | 921-937 | 17 | |
| α-helix | 938-940 | 3 | |
| α-helix | 950-961 | 12 | |
| β-strand | 964-968 | 5 | 13 |
| β-strand | 969 | 1 | 14 |
| β-strand | 977 | 1 | 15 |
| α-helix | 978-984 | 7 | |
| α-helix | 987-996 | 10 | |
| β-strand | 1000-1002 | 3 | 12 |
| β-strand | 1008-1010 | 3 | 12 |
| β-strand | 1013 | 1 | 15 |
| β-strand | 1017 | 1 | 16 |
| β-strand | 1019 | 1 | 16 |
| α-helix | 1022-1040 | 19 | |
| α-helix | 1045-1047 | 3 | |
| β-strand | 1049-1051 | 3 | 13 |
| β-strand | 1054-1058 | 5 | 13 |
| α-helix | 1062-1071 | 10 | |
| β-strand | 1076 | 1 | 14 |
| α-helix | 1078-1080 | 3 | |
| β-strand | 1082 | 1 | 13 |
| β-strand | 1087-1090 | 4 | 17 |
| β-strand | 1093-1096 | 4 | 17 |
| β-strand | 1099-1100 | 2 | 17 |
| α-helix | 1113-1127 | 15 | |
| β-strand | 1128 | 1 | 18 |
| β-strand | 1133 | 1 | 18 |
| α-helix | 1135-1144 | 10 | |
| α-helix | 1145-1147 | 3 | |
| α-helix | 1150-1153 | 4 | |
| β-strand | 1156-1157 | 2 | 19 |
| β-strand | 1166-1167 | 2 | 19 |
| β-strand | 1178 | 1 | 20 |
| β-strand | 1183-1195 | 13 | 20 |
| α-helix | 1199-1214 | 16 | |
| β-strand | 1247-1261 | 15 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicase | A | protein | 1289 | Escherichia coli O157:H7, synthetic construct, Escherichia phage Qbeta | P0A6N3 (AlphaFold model), P0A6P3 (AlphaFold model), P14647 |
| RNA (5'-r(*gp*gp*gp*up*cp*cp*a)-3') | G | RNA | 7 | ||
| RNA (5'-r(*ap*up*cp*gp*up*gp*gp*ap*cp*cp*cp*a)-3') | T | RNA | 12 |
>3AVU_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
>3AVU_2 RNA (5'-R(*GP*GP*GP*UP*CP*CP*A)-3') (chains G) GGGUCCA
>3AVU_3 RNA (5'-R(*AP*UP*CP*GP*UP*GP*GP*AP*CP*CP*CP*A)-3') (chains T) AUCGUGGACCCA
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
Molecular basis for RNA polymerization by Q beta replicase. Takeshita, D., Tomita, K. Nat Struct Mol Biol (2012) 19:229-237. DOI 10.1038/nsmb.2204 · PubMed
Other PDB entries of the same protein (UniProt P0A6N3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3AVU 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.