Structure of viral RNA polymerase complex 5. Determined by X-ray diffraction at 2.41 Å resolution. Released 18 Jan 2012.
Explore 3AVX in 3D Show helices and sheets RCSB PDB PDBe
3AVX contains 53 α-helices and 64 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 | 10-13 | 4 | |
| α-helix | 34-42 | 9 | |
| α-helix | 45-52 | 8 | |
| β-strand | 59-66 | 8 | 1 |
| β-strand | 70-78 | 9 | 1 |
| α-helix | 81-84 | 4 | |
| α-helix | 87-101 | 15 | |
| α-helix | 108-113 | 6 | |
| β-strand | 131-139 | 9 | 1 |
| β-strand | 142-148 | 7 | 2 |
| β-strand | 152-159 | 8 | 2 |
| α-helix | 163-176 | 14 | |
| β-strand | 180 | 1 | 3 |
| α-helix | 190-205 | 16 | |
| α-helix | 209-226 | 18 | |
| β-strand | 228 | 1 | 3 |
| β-strand | 233 | 1 | 4 |
| α-helix | 234 | 1 | |
| β-strand | 241 | 1 | 4 |
| α-helix | 242-247 | 6 | |
| β-strand | 252-260 | 9 | 2 |
| α-helix | 272-284 | 13 | |
| α-helix | 294-295 | 2 | |
| β-strand | 296-303 | 8 | 5 |
| α-helix | 309-323 | 15 | |
| β-strand | 352-355 | 4 | 5 |
| β-strand | 360-365 | 6 | 5 |
| α-helix | 369-378 | 10 | |
| β-strand | 385-391 | 7 | 5 |
| α-helix | 400-410 | 11 | |
| β-strand | 415-420 | 6 | 5 |
| α-helix | 428-444 | 17 | |
| β-strand | 454-456 | 3 | 5 |
| α-helix | 467-482 | 16 | |
| α-helix | 485-489 | 5 | |
| α-helix | 490-492 | 3 | |
| α-helix | 494-495 | 2 | |
| β-strand | 496-498 | 3 | 6 |
| β-strand | 501-505 | 5 | 7 |
| β-strand | 509-515 | 7 | 7 |
| β-strand | 518 | 1 | 6 |
| β-strand | 520-522 | 3 | 8 |
| β-strand | 526-530 | 5 | 6 |
| β-strand | 536-539 | 4 | 6 |
| β-strand | 540-544 | 5 | 7 |
| β-strand | 549-550 | 2 | 7 |
| β-strand | 552-554 | 3 | 8 |
| β-strand | 558-563 | 6 | 7 |
| α-helix | 568-570 | 3 | |
| β-strand | 573 | 1 | 9 |
| β-strand | 575 | 1 | 9 |
| β-strand | 576-578 | 3 | 6 |
| β-strand | 585-595 | 11 | 10 |
| α-helix | 598-600 | 3 | |
| β-strand | 607 | 1 | 11 |
| β-strand | 614-616 | 3 | 10 |
| β-strand | 621-627 | 7 | 10 |
| α-helix | 628-629 | 2 | |
| β-strand | 635 | 1 | 11 |
| β-strand | 642-652 | 11 | 10 |
| β-strand | 658-663 | 6 | 10 |
| β-strand | 666-676 | 11 | 10 |
| α-helix | 703-713 | 11 | |
| α-helix | 723-734 | 12 | |
| α-helix | 745-747 | 3 | |
| α-helix | 757-769 | 13 | |
| α-helix | 784-804 | 21 | |
| α-helix | 817-833 | 17 | |
| α-helix | 839-845 | 7 | |
| α-helix | 858-860 | 3 | |
| α-helix | 863-868 | 6 | |
| α-helix | 870 | 1 | |
| β-strand | 871-873 | 3 | 12 |
| α-helix | 878-885 | 8 | |
| β-strand | 894-897 | 4 | 12 |
| β-strand | 900-906 | 7 | 13 |
| β-strand | 914-918 | 5 | 13 |
| α-helix | 919-920 | 2 | |
| α-helix | 921-938 | 18 | |
| α-helix | 939-941 | 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 | 978-982 | 5 | |
| α-helix | 987-996 | 10 | |
| β-strand | 1000-1002 | 3 | 13 |
| β-strand | 1008-1010 | 3 | 13 |
| β-strand | 1013 | 1 | 16 |
| β-strand | 1017 | 1 | 17 |
| β-strand | 1019 | 1 | 17 |
| α-helix | 1022-1040 | 19 | |
| 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 |
| α-helix | 1078-1080 | 3 | |
| β-strand | 1082 | 1 | 14 |
| β-strand | 1087-1090 | 4 | 18 |
| β-strand | 1093-1096 | 4 | 18 |
| β-strand | 1099-1100 | 2 | 18 |
| α-helix | 1113-1127 | 15 | |
| β-strand | 1128-1129 | 2 | 19 |
| β-strand | 1132-1133 | 2 | 19 |
| α-helix | 1135-1145 | 11 | |
| α-helix | 1150-1154 | 5 | |
| β-strand | 1156-1157 | 2 | 20 |
| β-strand | 1166-1167 | 2 | 20 |
| α-helix | 1176 | 1 | |
| β-strand | 1177-1179 | 3 | 21 |
| β-strand | 1182-1194 | 13 | 21 |
| α-helix | 1199-1214 | 16 | |
| α-helix | 1237-1239 | 3 | |
| β-strand | 1248-1260 | 13 | 21 |
| 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(*gp*gp*gp*up*cp*cp*ap*up*c)-3') | G | RNA | 9 | ||
| RNA (5'-r(*ap*ap*cp*gp*ap*up*gp*gp*ap*cp*cp*cp*a)-3') | T | RNA | 13 |
>3AVX_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
>3AVX_2 RNA (5'-R(*GP*GP*GP*UP*CP*CP*AP*UP*C)-3') (chains G) GGGUCCAUC
>3AVX_3 RNA (5'-R(*AP*AP*CP*GP*AP*UP*GP*GP*AP*CP*CP*CP*A)-3') (chains T) AACGAUGGACCCA
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:
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