Cryo-EM structure of CVA10 empty particle. Determined by electron microscopy at 2.7 Å resolution. Released 16 Jan 2019.
Explore 6AKU in 3D Show helices and sheets RCSB PDB PDBe
6AKU contains 23 α-helices and 46 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 76-78 | 3 | |
| β-strand | 79 | 1 | 1 |
| α-helix | 80-83 | 4 | |
| β-strand | 88-97 | 10 | 2 |
| β-strand | 98 | 1 | 3 |
| β-strand | 100 | 1 | 3 |
| β-strand | 105-109 | 5 | 4 |
| α-helix | 118-122 | 5 | |
| β-strand | 125-139 | 15 | 2 |
| β-strand | 149-155 | 7 | 4 |
| α-helix | 160-162 | 3 | |
| α-helix | 168-171 | 4 | |
| β-strand | 177-181 | 5 | 4 |
| α-helix | 185-186 | 2 | |
| β-strand | 187-191 | 5 | 2 |
| β-strand | 200-201 | 2 | 2 |
| β-strand | 206 | 1 | 5 |
| β-strand | 231-236 | 6 | 4 |
| α-helix | 241-243 | 3 | |
| β-strand | 244-262 | 19 | 2 |
| α-helix | 264-266 | 3 | |
| β-strand | 272 | 1 | 6 |
| β-strand | 275 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31-33 | 3 | 7 |
| α-helix | 41-43 | 3 | |
| β-strand | 64-65 | 2 | 7 |
| α-helix | 67-68 | 2 | |
| β-strand | 69-71 | 3 | 7 |
| β-strand | 78-82 | 5 | 8 |
| α-helix | 84-86 | 3 | |
| α-helix | 92-96 | 5 | |
| β-strand | 102 | 1 | 9 |
| β-strand | 103-112 | 10 | 7 |
| β-strand | 119-128 | 10 | 8 |
| α-helix | 149-152 | 4 | |
| β-strand | 159-160 | 2 | 8 |
| α-helix | 164-166 | 3 | |
| α-helix | 173-178 | 6 | |
| β-strand | 181-185 | 5 | 8 |
| β-strand | 191-196 | 6 | 7 |
| β-strand | 205 | 1 | 9 |
| β-strand | 210 | 1 | 5 |
| β-strand | 213-224 | 12 | 8 |
| β-strand | 233-245 | 13 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23 | 1 | 2 |
| α-helix | 31-33 | 3 | |
| β-strand | 39 | 1 | 2 |
| β-strand | 42 | 1 | 1 |
| α-helix | 43-47 | 5 | |
| β-strand | 51-52 | 2 | 10 |
| α-helix | 64-67 | 4 | |
| β-strand | 69-72 | 4 | 10 |
| β-strand | 80-86 | 7 | 11 |
| α-helix | 98-103 | 6 | |
| β-strand | 106-111 | 6 | 12 |
| β-strand | 113-120 | 8 | 10 |
| β-strand | 126 | 1 | 13 |
| β-strand | 128-134 | 7 | 11 |
| α-helix | 139-141 | 3 | |
| α-helix | 144-148 | 5 | |
| β-strand | 152-156 | 5 | 11 |
| β-strand | 162-165 | 4 | 10 |
| β-strand | 170-171 | 2 | 12 |
| α-helix | 174-177 | 4 | |
| β-strand | 190-196 | 7 | 11 |
| α-helix | 199-200 | 2 | |
| β-strand | 201 | 1 | 13 |
| β-strand | 209-218 | 10 | 10 |
| β-strand | 223-227 | 5 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| VP1 | A | protein | 298 | Coxsackievirus A10 | W0G0K3 |
| VP2 | B | protein | 255 | Coxsackievirus A10 | A0A0C5AZ80 |
| VP3 | C | protein | 240 | Coxsackievirus A10 | A0A0C5AWF6 |
>6AKU_1 VP1 (chains A) GDPVEDIIHDALGSTARRAISSATNVESAANTTPSSHRLETGRVPALQAAETGATSNATD ENMIETRCVVNRNGVLETTINHFFSRSGLVGVVNLTDGGTDTTGYVTWDIDIMGFVQLRR KCEMFTYMRFNAEFTFVTTTKNGEARPYMLQYMYVPPGAPKPTGRDAFQWQTATNPSVFV KLTDPPAQVSVPFMSPASAYQWFYDGYPTFGQHPETSNTTYGLCPNNMMGTFAVRVVSRE ASQLKLQTRVYMKLKHVRAWVPRPIRSQPYLLKNFPNYDSSKITNSARDRSSIKQANM
>6AKU_2 VP2 (chains B) SPSVEACGYSDRVAQLTVGNSSITTQEAANIVLAYGEWPEYCPDTDATAVDKPTRPDVSV NRFYTLDSKMWQENSTGWYWKFPDVLNKTGVFGQNAQFHYLYRSGFCLHVQCNASKFHQG ALLVAVIPEFVIAGRGSNTKPNEAPHPGFTTTFPGTTGATFHDPYVLDSGVPLSQALIYP HQWINLRTNNCATVIVPYINAVPFDSAINHSNFGLIVIPVSPLKYSSGATTAIPITITIA PLNSEFGGLRQAVSQ
>6AKU_3 VP3 (chains C) GIPAELRPGTNQFLTTDDDTAAPILPGFTPTPTIHIPGEVHSLLELCRVETILEVNNTTE ATGLTRLLIPVSSQNKADELCAAFMVDPGRIGPWQSTLVGQICRYYTQWSGSLKVTFMFT GSFMATGKMLVAYSPPGSAQPANRETAMLGTHVIWDFGLQSSVSLVIPWISNTHFRTAKT GGNYDYYTAGVVTLWYQTNYVVPPETPGEAYIIAMGADLYKFTLKICKDTDEVTQQAVLQ
Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating. Zhu, L., Sun, Y., Fan, J. et al. Nat Commun (2018) 9:4985-4985. DOI 10.1038/s41467-018-07531-0 · PubMed
Other PDB entries of the same protein (UniProt W0G0K3), best resolution first:
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