Cryo-EM structure of echovirus 11 empty particle at pH 7.4. Determined by electron microscopy at 3.18 Å resolution. Released 7 Oct 2020.
Explore 6LBO in 3D Show helices and sheets RCSB PDB PDBe
6LBO contains 20 α-helices and 51 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 |
|---|---|---|---|
| β-strand | 63 | 1 | 1 |
| α-helix | 64-68 | 5 | |
| β-strand | 72-80 | 9 | 2 |
| β-strand | 91-94 | 4 | 3 |
| α-helix | 101-107 | 7 | |
| β-strand | 110-127 | 18 | 2 |
| α-helix | 138-140 | 3 | |
| β-strand | 141-147 | 7 | 3 |
| α-helix | 160-163 | 4 | |
| β-strand | 169-173 | 5 | 3 |
| α-helix | 177-179 | 3 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 192-193 | 2 | 2 |
| β-strand | 198 | 1 | 4 |
| β-strand | 199 | 1 | 5 |
| β-strand | 208 | 1 | 5 |
| α-helix | 212-214 | 3 | |
| β-strand | 218-223 | 6 | 3 |
| α-helix | 229-231 | 3 | |
| β-strand | 232-250 | 19 | 2 |
| α-helix | 252-254 | 3 | |
| α-helix | 257-258 | 2 | |
| α-helix | 282-284 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 6 |
| β-strand | 21-25 | 5 | 6 |
| β-strand | 31-33 | 3 | 7 |
| β-strand | 53-54 | 2 | 7 |
| β-strand | 64-65 | 2 | 7 |
| β-strand | 69-71 | 3 | 7 |
| β-strand | 78-82 | 5 | 8 |
| α-helix | 90-98 | 9 | |
| β-strand | 102-112 | 11 | 7 |
| β-strand | 119-128 | 10 | 8 |
| β-strand | 134 | 1 | 9 |
| β-strand | 148 | 1 | 10 |
| β-strand | 151 | 1 | 10 |
| α-helix | 152 | 1 | |
| β-strand | 153-154 | 2 | 8 |
| β-strand | 156 | 1 | 11 |
| β-strand | 166 | 1 | 9 |
| β-strand | 169 | 1 | 11 |
| α-helix | 179-184 | 6 | |
| β-strand | 187-191 | 5 | 8 |
| β-strand | 197-202 | 6 | 7 |
| β-strand | 211 | 1 | 7 |
| β-strand | 216 | 1 | 4 |
| β-strand | 219-230 | 12 | 8 |
| β-strand | 239-253 | 15 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 23 | 1 | 2 |
| α-helix | 29-34 | 6 | |
| β-strand | 39-40 | 2 | 2 |
| β-strand | 42 | 1 | 1 |
| α-helix | 44-47 | 4 | |
| β-strand | 51-52 | 2 | 12 |
| α-helix | 65-68 | 4 | |
| β-strand | 70-72 | 3 | 12 |
| β-strand | 81-86 | 6 | 13 |
| α-helix | 99-104 | 6 | |
| β-strand | 107-111 | 5 | 14 |
| β-strand | 112-120 | 9 | 12 |
| β-strand | 127 | 1 | 15 |
| β-strand | 129-135 | 7 | 13 |
| α-helix | 140-142 | 3 | |
| α-helix | 145-149 | 5 | |
| β-strand | 152-157 | 6 | 13 |
| β-strand | 163-171 | 9 | 12 |
| β-strand | 189-194 | 6 | 13 |
| β-strand | 199 | 1 | 15 |
| β-strand | 208-216 | 9 | 12 |
| β-strand | 221-225 | 5 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Capsid protein VP1 | A | protein | 226 | Echovirus E11 | Q2LJ73 |
| Capsid protein VP2 | B | protein | 245 | Echovirus E11 | A0A0R5YS56 |
| Capsid protein VP3 | C | protein | 231 | Echovirus E11 | A8ILJ7 |
>6LBO_1 Capsid protein VP1 (chains A) SESSIENFLCRSACVYMGEYHTTNTDTSKLFASWTINARRMVQMRRKLELFTYVRFDMEV TFVITSKQDQGTQLGQDMPPLTHQIMYIPPGGPIPKSVTDYTWQTSTNPSIFWTEGNAPP RMSIPFISIGNAYSNFYDGWSHFSQNGVYGYNTLNHMGQIYVRHVNGSSPLPMTSTVRMY FKPKHVKVWVPRPPRLCQYKNASTVNFTPTNITEKRQSINYIPETV
>6LBO_2 Capsid protein VP2 (chains B) RVRSITLGNSTITTQESANVVVAYGRWPEYLKDNEATAEDQPTQPDVATCRFYTLESVTW ERDSPGWWWKFPDALKDMGLFGQNMYYHYLGRAGYTIHVQCNASKFHQGCLMVVCVPEAE MGCSQVDGTVNEHSLSEGETAKKFASTSTNGTNTVQSIVTNAGMGVGVGNLTIFPHQWIN LRTNNCATIVMPYINNVPMDNMFRHHNFTLMIIPFVPLDYSSDSSTYVPITVTVAPMCAE YNGLR
>6LBO_3 Capsid protein VP3 (chains C) GLPVMNTPGSNQFLTSDDFQSPSAMPQFDVTPELNIPGEVQNLMEIAEVDSVVPVNNVEG KLDTMEIYRIPVQSGNHQSSQVFGFQVQPGLDNVFKHTLLGEILNYYAHWSGSIKLTFVF CGSAMATGKFLLAYAPPGANAPKSRKDAMLGTHIIWDVGLQSSCVLCIPWISQTHYRLVQ QDEYTSAGNVTCWYQTGIVVPAGTPTSCSIMCFVSACNDFSVRLLKDTPFI
Molecular and structural basis of Echovirus 11 infection by using the dual-receptor system of CD55 and FcRn. Niu, S., Liu, C., Liu, C. et al. Chin Sci Bull (2020). DOI 10.1360/TB-2019-0786
Other PDB entries of the same protein (UniProt Q2LJ73), best resolution first:
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