3VNV: Complex structure of viral RNA polymerase II

Complex structure of viral RNA polymerase II. Determined by X-ray diffraction at 2.6 Å resolution. Released 8 Aug 2012.

Method
X-ray diffraction
Resolution
2.6 Å
Organisms
Escherichia coli O157:H7, Escherichia phage Qbeta
Chains
3
Atoms
9,680
Mol. weight
146.74 kDa
Ligands
CH1, CA
Released
8 Aug 2012

Explore 3VNV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VNV contains 59 α-helices and 62 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.

Chain A: 59 helices, 62 β-strands

ElementResiduesLengthSheet
α-helix6-149
α-helix20-289
α-helix34-429
α-helix45-495
β-strand59-6791
β-strand70-7891
α-helix81-844
α-helix87-10115
α-helix108-1136
α-helix116-12611
β-strand131-13991
β-strand142-14872
β-strand152-15982
α-helix163-17614
β-strand18013
α-helix183-1853
α-helix195-2039
α-helix209-22618
β-strand22813
α-helix229-2313
β-strand23314
β-strand24114
α-helix242-2476
β-strand252-26092
α-helix273-2808
α-helix281-2833
β-strand296-30385
α-helix309-32214
β-strand352-35655
β-strand359-36575
α-helix369-3779
β-strand385-39175
α-helix400-41011
β-strand415-42065
α-helix422-4243
α-helix428-44417
α-helix449-4513
β-strand454-45635
α-helix459-4635
α-helix470-48314
α-helix485-4873
α-helix490-4923
α-helix494-4952
β-strand496-49836
β-strand501-50447
β-strand510-51567
β-strand51816
β-strand520-52238
β-strand526-53056
β-strand536-53946
β-strand540-54457
β-strand549-55027
β-strand552-55438
β-strand558-56367
α-helix568-5703
β-strand57319
β-strand57519
β-strand576-57836
β-strand585-5951110
β-strand607111
β-strand614-616310
β-strand621-627710
β-strand635111
β-strand640-6521310
β-strand658-663610
β-strand666-6761110
α-helix703-71311
α-helix723-73412
α-helix743-7464
α-helix757-76812
α-helix784-80421
α-helix817-83317
α-helix839-8457
α-helix858-8603
α-helix863-8664
α-helix8701
β-strand871-873312
α-helix875-8773
α-helix878-8858
β-strand894-897412
β-strand900-9091013
β-strand912-918713
α-helix919-9202
α-helix921-93717
α-helix938-9414
α-helix949-96113
β-strand964-967414
β-strand969115
α-helix972-9743
β-strand977116
α-helix978-9847
α-helix987-99610
β-strand1000-1002313
β-strand1008-1010313
β-strand1013116
α-helix1022-104019
α-helix1045-10473
β-strand1049-1051314
β-strand1054-1058514
α-helix1059-10613
α-helix1062-107110
β-strand1076115
β-strand1082114
β-strand1087-1090417
β-strand1093-1096417
β-strand1099-1100217
α-helix1113-112715
β-strand1128-1129218
β-strand1132-1133218
α-helix11341
α-helix1135-114511
α-helix1150-11545
β-strand1156-1157219
β-strand1166-1167219
α-helix1170-11723
β-strand1177-1179320
β-strand1182-11941320
α-helix1199-121416
α-helix1237-12393
α-helix1243-12453
β-strand1248-12611420

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicaseAprotein1289Escherichia coli O157:H7, Escherichia phage QbetaP0A6N3 (AlphaFold model), P0A6P3 (AlphaFold model), P14647
RNA (5'-r(*cp*cp*cp*up*ap*cp*c)-3')GRNA7
RNA (5'-r(*gp*gp*gp*up*ap*gp*gp*g)-3')TRNA8
Sequence of entity 1 (A), FASTA
>3VNV_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
Sequence of entity 2 (G), FASTA
>3VNV_2 RNA (5'-R(*CP*CP*CP*UP*AP*CP*C)-3') (chains G)
CCCUACC
Sequence of entity 3 (T), FASTA
>3VNV_3 RNA (5'-R(*GP*GP*GP*UP*AP*GP*GP*G)-3') (chains T)
GGGUAGGG

Ligands and cofactors

IDNameFormulaCopies
CH13'-deoxy-cytidine-5'-triphosphateC9 H16 N3 O13 P31
CACalcium ionCa2

Primary citation

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:

Browse structure collections

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