Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. Determined by X-ray diffraction at 2.88 Å resolution. Released 17 Oct 1989.
Explore 2PLV in 3D Show helices and sheets RCSB PDB PDBe
2PLV contains 29 α-helices and 64 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 8-9 | 2 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 26 | 1 | 3 |
| α-helix | 27-29 | 3 | |
| β-strand | 30 | 1 | 4 |
| β-strand | 44-45 | 2 | 5 |
| α-helix | 47-49 | 3 | |
| α-helix | 57-59 | 3 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66 | 1 | 4 |
| β-strand | 71 | 1 | 3 |
| α-helix | 73-75 | 3 | |
| β-strand | 76 | 1 | 6 |
| α-helix | 77-81 | 5 | |
| β-strand | 85-94 | 10 | 7 |
| β-strand | 106-109 | 4 | 8 |
| α-helix | 117-122 | 6 | |
| β-strand | 125-142 | 18 | 7 |
| β-strand | 154-160 | 7 | 8 |
| α-helix | 173-176 | 4 | |
| β-strand | 182-186 | 5 | 8 |
| β-strand | 192-196 | 5 | 7 |
| β-strand | 205-206 | 2 | 7 |
| β-strand | 211 | 1 | 9 |
| β-strand | 217 | 1 | 10 |
| α-helix | 222-225 | 4 | |
| β-strand | 239-244 | 6 | 8 |
| β-strand | 253-271 | 19 | 7 |
| α-helix | 295-296 | 2 | |
| β-strand | 297 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 12 |
| β-strand | 21-25 | 5 | 12 |
| β-strand | 28-33 | 6 | 13 |
| α-helix | 34-36 | 3 | |
| β-strand | 54 | 1 | 13 |
| α-helix | 57-59 | 3 | |
| β-strand | 64-65 | 2 | 13 |
| α-helix | 66-68 | 3 | |
| β-strand | 69-72 | 4 | 14 |
| β-strand | 78-82 | 5 | 15 |
| α-helix | 84-86 | 3 | |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 13 |
| β-strand | 118-128 | 11 | 15 |
| α-helix | 131-133 | 3 | |
| β-strand | 134 | 1 | 16 |
| α-helix | 145-148 | 4 | |
| α-helix | 151-153 | 3 | |
| β-strand | 155-156 | 2 | 15 |
| β-strand | 158 | 1 | 17 |
| β-strand | 174 | 1 | 16 |
| β-strand | 177 | 1 | 17 |
| α-helix | 178-180 | 3 | |
| α-helix | 187-192 | 6 | |
| β-strand | 195-199 | 5 | 15 |
| β-strand | 205-210 | 6 | 13 |
| β-strand | 219 | 1 | 13 |
| β-strand | 224 | 1 | 9 |
| β-strand | 227-239 | 13 | 15 |
| β-strand | 246-249 | 4 | 14 |
| β-strand | 250-263 | 14 | 13 |
| β-strand | 269 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23 | 1 | 7 |
| β-strand | 39-40 | 2 | 7 |
| β-strand | 42 | 1 | 6 |
| α-helix | 43-47 | 5 | |
| β-strand | 51-52 | 2 | 5 |
| β-strand | 57 | 1 | 11 |
| α-helix | 65-68 | 4 | |
| β-strand | 70-73 | 4 | 5 |
| β-strand | 83-86 | 4 | 18 |
| α-helix | 99-104 | 6 | |
| β-strand | 107-111 | 5 | 19 |
| β-strand | 114-120 | 7 | 5 |
| β-strand | 127 | 1 | 20 |
| β-strand | 129-135 | 7 | 18 |
| α-helix | 145-149 | 5 | |
| β-strand | 152-157 | 6 | 18 |
| β-strand | 163-168 | 6 | 5 |
| β-strand | 177-178 | 2 | 19 |
| α-helix | 183-185 | 3 | |
| β-strand | 189-194 | 6 | 18 |
| β-strand | 199 | 1 | 20 |
| β-strand | 207-216 | 10 | 5 |
| β-strand | 221-225 | 5 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 26-29 | 4 | 1 |
| α-helix | 36-38 | 3 | |
| α-helix | 45 | 1 | |
| β-strand | 46 | 1 | 2 |
| α-helix | 47 | 1 | |
| α-helix | 51-54 | 4 | |
| β-strand | 57 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human poliovirus type 1 (subunit VP1) | 1 | protein | 302 | Human poliovirus 1 | P03300 (AlphaFold model) |
| Human poliovirus type 1 (subunit VP2) | 2 | protein | 272 | Human poliovirus 1 | P03300 (AlphaFold model) |
| Human poliovirus type 1 (subunit VP3) | 3 | protein | 238 | Human poliovirus 1 | P03300 (AlphaFold model) |
| Human poliovirus type 1 (subunit VP4) | 4 | protein | 68 | Human poliovirus 1 | P03300 (AlphaFold model) |
>2PLV_1 HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP1) (chains 1) GLGQMLESMIDNTVSSTVGAATSRDALPNTEASGPTHSKEIPALTAVETGATNPLVPSDT VQTRHVVQHRSRSESSIESFFARGACVTIMTVDNPASTTNKDKLFAVWKITYKDTVQLRR KLEFFTYSRFDMELTFVVTANFTETNNGHALNQVYQIMYVPPGAPVPEKWDDYTWQTSSN PSIFYTYGTAPARISVPYVGISNAYSHFYDGFSKVPLKDQSAALGDSLYGAASLNDFGIL AVRVVNDHNPTKVTSKIRVYLKPKHIRVWCPRPPRAVAYYGPGVDYKDGTLTPLSTKDLT TY
>2PLV_2 HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP2) (chains 2) SPNIEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEYLRDSEANPVDQPTEPDVAA CRFYTLDTVSWTKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQG ALGVFAVPEMCLAGDSNTTTMHTSYQNANPGEKGGTFTGTFTPDNNQTSPARRFCPVDYL LGNGTLLGNAFVFPHQIINLRTNNCATLVLPYVNSLSIDSMVKHNNWGIAILPLAPLNFA SESSPEIPITLTIAPMCCEFNGLRNITLPRLQ
>2PLV_3 HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP3) (chains 3) GLPVMNTPGSNQYLTADNFQSPCALPEFDVTPPIDIPGEVKNMMELAEIDTMIPFDLSAT KKNTMEMYRVRLSDKPHTDDPILCLSLSPASDPRLSHTMLGEILNYYTHWAGSLKFTFLF CGSMMATGKLLVSYAPPGADPPKKRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTI DDSFTEGGYISVFYQTRIVVPLSTPREMDILGFVSACNDFSVRLLRDTTHIEQKALAQ
>2PLV_4 HUMAN POLIOVIRUS TYPE 1 (SUBUNIT VP4) (chains 4) GAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFSQDPSKFTEPIKDVL IKTAPMLN
Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. Filman, D.J., Syed, R., Chow, M. et al. EMBO J (1989) 8:1567-1579. PubMed
Other PDB entries of the same protein (UniProt P03300 (AlphaFold model), which also has an AlphaFold model), best resolution first:
2PLV is part of these collections:
MolViewer shows 2PLV 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.