Coxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1. Determined by electron microscopy at 3.9 Å resolution. Released 10 Jan 2018.
Explore 6EIT in 3D Show helices and sheets RCSB PDB PDBe
6EIT contains 26 α-helices and 71 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 | 30 | 1 | 1 |
| β-strand | 33 | 1 | 2 |
| α-helix | 47-49 | 3 | |
| α-helix | 57-60 | 4 | |
| β-strand | 63 | 1 | 2 |
| β-strand | 66 | 1 | 1 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-86 | 2 | 3 |
| β-strand | 90-94 | 5 | 4 |
| β-strand | 107-111 | 5 | 5 |
| α-helix | 120-124 | 5 | |
| β-strand | 127-137 | 11 | 6 |
| β-strand | 138-144 | 7 | 4 |
| β-strand | 156-162 | 7 | 5 |
| β-strand | 164 | 1 | 7 |
| β-strand | 166 | 1 | 7 |
| α-helix | 167-169 | 3 | |
| α-helix | 175-178 | 4 | |
| β-strand | 184-188 | 5 | 5 |
| α-helix | 192-194 | 3 | |
| β-strand | 195-198 | 4 | 6 |
| β-strand | 207-208 | 2 | 6 |
| β-strand | 213 | 1 | 8 |
| β-strand | 219 | 1 | 9 |
| β-strand | 229 | 1 | 10 |
| α-helix | 230-231 | 2 | |
| α-helix | 232-235 | 4 | |
| β-strand | 241-246 | 6 | 5 |
| β-strand | 255-261 | 7 | 4 |
| β-strand | 262-263 | 2 | 3 |
| β-strand | 264-273 | 10 | 6 |
| α-helix | 275-277 | 3 | |
| α-helix | 280-281 | 2 | |
| α-helix | 290-292 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 11 |
| β-strand | 21-25 | 5 | 11 |
| β-strand | 32-33 | 2 | 12 |
| α-helix | 34-36 | 3 | |
| α-helix | 41-43 | 3 | |
| α-helix | 44-46 | 3 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54 | 1 | 12 |
| β-strand | 64-65 | 2 | 12 |
| β-strand | 69-71 | 3 | 13 |
| β-strand | 78-81 | 4 | 14 |
| α-helix | 82-85 | 4 | |
| α-helix | 92-97 | 6 | |
| β-strand | 99-111 | 13 | 12 |
| β-strand | 121-128 | 8 | 14 |
| β-strand | 134 | 1 | 15 |
| β-strand | 155-156 | 2 | 14 |
| β-strand | 158 | 1 | 16 |
| β-strand | 173 | 1 | 15 |
| β-strand | 176 | 1 | 16 |
| α-helix | 186-191 | 6 | |
| β-strand | 195-198 | 4 | 14 |
| β-strand | 204-209 | 6 | 12 |
| β-strand | 218 | 1 | 12 |
| β-strand | 223 | 1 | 8 |
| β-strand | 226-232 | 7 | 14 |
| β-strand | 246-248 | 3 | 13 |
| β-strand | 249-262 | 14 | 12 |
| α-helix | 265-266 | 2 | |
| β-strand | 268 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 13-14 | 2 | 5 |
| α-helix | 30-33 | 4 | |
| α-helix | 43-45 | 3 | |
| β-strand | 51-52 | 2 | 17 |
| β-strand | 70-72 | 3 | 18 |
| β-strand | 83-85 | 3 | 19 |
| α-helix | 98-103 | 6 | |
| β-strand | 108-110 | 3 | 20 |
| β-strand | 113-119 | 7 | 18 |
| β-strand | 126-134 | 9 | 19 |
| α-helix | 139-141 | 3 | |
| α-helix | 144-147 | 4 | |
| β-strand | 151-156 | 6 | 19 |
| β-strand | 162-167 | 6 | 18 |
| β-strand | 176-177 | 2 | 20 |
| β-strand | 188-198 | 11 | 19 |
| β-strand | 207-211 | 5 | 18 |
| β-strand | 212-213 | 2 | 17 |
| β-strand | 214-215 | 2 | 18 |
| β-strand | 220-222 | 3 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 21 |
| β-strand | 8-10 | 3 | 22 |
| β-strand | 17-20 | 4 | 23 |
| β-strand | 21-23 | 3 | 21 |
| β-strand | 30 | 1 | 10 |
| β-strand | 31-34 | 4 | 24 |
| β-strand | 39 | 1 | 23 |
| β-strand | 42 | 1 | 23 |
| β-strand | 51-54 | 4 | 23 |
| β-strand | 64-67 | 4 | 24 |
| β-strand | 77 | 1 | 24 |
| β-strand | 79-81 | 3 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| VP1 | 1 | protein | 305 | Coxsackievirus A24 | V9VEF3 |
| VP2 | 2 | protein | 271 | Coxsackievirus A24 | V9VEF3 |
| VP3 | 3 | protein | 240 | Coxsackievirus A24 | V9VEF3 |
| Intercellular adhesion molecule 1 | 4 | protein | 85 | Homo sapiens | P05362 (AlphaFold model) |
>6EIT_1 VP1 (chains 1) GIEETIDTVITNALQLSQPKPQKQPTAQSTPLTSGVNSQEVPALTAVETGASGQAVPSDV IETRHVVNYKTRSESTLESFFGRSACVTILEVENFNATTDADRKKQFTTWAITYTDTVQL RRKLEFFTYSRFDLEMTFVITERYYASNTGHARNQVYQLMYIPPGAPRPTAWDDYTWQSS SNPSVFYTYGSAPPRMSIPYVGIANAYSHFYDGFARVPLKDETVDSGDTYYGLVTINDFG TLAVRVVNEYNPARITSKIRVYMKPKHVRCWCPRPPRAVPYRGEGVDFKQDSITPLTAVE NINTF
>6EIT_2 VP2 (chains 2) SPNVEACGYSDRVRQITLGNSTITTQEAANAVVAYGEWPSYLDDKEANPIDAPTEPDVSS NRFYTLDSVQWKSTSRGWWWKLPDALKDMGMFGQNMYYHYLGRSGYTVHVQCNASKFHQG ALGVFAIPEYVMACNTEAKTSYVSYVNANPGEKGGVFDNAYNPSAEASEGRKFAALDYLL GCGVLAGNAFVYPHQIINLRTNNSATLVLPYVNSLAIDCMAKHNNWGLVILPLCKLDYAP NSSTEIPITVTIAPMFTEFNGLRNITVPATQ
>6EIT_3 VP3 (chains 3) GLPTMLTPGSSQFLTSDDFQSPCALPNFDVTPPIHIPGEVFNMMELAEIDSMIPMNSVTG KANTMEMYPIPLDDKGSATPIFSISLSPASDKRLQYTMLGEILNYYTHWTGSLRFTFLFC GSMMATGKILLSYSPPGAKPPTTRKDAMLGTHIIWDLGLQSSCTMLAPWISNTVYRRCIK DDFTEGGYITCFYQTRIVVPSGTPTSMFMLAFVSACPDFSVRLLRDTNHISQRTLFARAQ
>6EIT_4 Intercellular adhesion molecule 1 (chains 4) QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQED SQPMCYSNCPDGQSTAKTFLTVYWT
Role of enhanced receptor engagement in the evolution of a pandemic acute hemorrhagic conjunctivitis virus. Baggen, J., Hurdiss, D.L., Zocher, G. et al. Proc Natl Acad Sci U S A (2018) 115:397-402. DOI 10.1073/pnas.1713284115 · PubMed
Other PDB entries of the same protein (UniProt V9VEF3), best resolution first:
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