8YW1: Semliki Forest virus viron
Semliki Forest virus viron in complex with VLDLR. Determined by electron microscopy at 3.44 Å resolution. Released 11 Dec 2024.
- Method
- Electron microscopy
- Resolution
- 3.44 Å
- Organisms
- Semliki Forest virus 4, Homo sapiens
- Chains
- 33
- Atoms
- 67,744
- Mol. weight
- 967.94 kDa
- Released
- 11 Dec 2024
Explore 8YW1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8YW1 contains 217 α-helices and 740 β-strands across 33 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.
Chains a and L: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-30 | 4 | |
| α-helix | 32-39 | 8 | |
| α-helix | 49-55 | 7 | |
Chains A and E: 12 helices, 41 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-8 | 7 | 1 |
| β-strand | 15-19 | 5 | 2 |
| β-strand | 24 | 1 | 3 |
| β-strand | 27-48 | 22 | 2 |
| β-strand | 51-54 | 4 | 4 |
| α-helix | 56-58 | 3 | |
| β-strand | 59-61 | 3 | 5 |
| β-strand | 77-82 | 6 | 5 |
| β-strand | 101-106 | 6 | 5 |
| β-strand | 107-110 | 4 | 4 |
| β-strand | 119-136 | 18 | 2 |
| β-strand | 137 | 1 | 6 |
| β-strand | 140 | 1 | 6 |
| β-strand | 143-147 | 5 | 2 |
| β-strand | 152 | 1 | 7 |
| β-strand | 153-156 | 4 | 1 |
| β-strand | 159-163 | 5 | 1 |
| α-helix | 164-166 | 3 | |
| β-strand | 176-180 | 5 | 2 |
| β-strand | 183-186 | 4 | 2 |
| α-helix | 189-191 | 3 | |
| β-strand | 192 | 1 | 8 |
| α-helix | 195-196 | 2 | |
| β-strand | 203-204 | 2 | 9 |
| β-strand | 205 | 1 | 2 |
| β-strand | 214-215 | 2 | 9 |
| β-strand | 220-221 | 2 | 10 |
| α-helix | 223-225 | 3 | |
| β-strand | 233-234 | 2 | 10 |
| α-helix | 236-238 | 3 | |
| α-helix | 239-245 | 7 | |
| α-helix | 256-258 | 3 | |
| β-strand | 260-262 | 3 | 2 |
| β-strand | 267-269 | 3 | 2 |
| β-strand | 275-281 | 7 | 1 |
| α-helix | 284-286 | 3 | |
| β-strand | 289 | 1 | 3 |
| α-helix | 294-295 | 2 | |
| β-strand | 296-306 | 11 | 11 |
| β-strand | 307 | 1 | 12 |
| β-strand | 314-322 | 9 | 11 |
| β-strand | 326-329 | 4 | 13 |
| β-strand | 330-332 | 3 | 14 |
| β-strand | 337-339 | 3 | 15 |
| β-strand | 343-346 | 4 | 13 |
| β-strand | 351-355 | 5 | 11 |
| β-strand | 356-358 | 3 | 15 |
| β-strand | 364-369 | 6 | 14 |
| β-strand | 374-377 | 4 | 14 |
| β-strand | 381 | 1 | 12 |
| β-strand | 387-388 | 2 | 16 |
| α-helix | 399-401 | 3 | |
| α-helix | 405-437 | 33 | |
Chains b and M: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9 | 1 | 27 |
| β-strand | 16 | 1 | 27 |
| α-helix | 27-30 | 4 | |
| α-helix | 32-41 | 10 | |
| α-helix | 48-55 | 8 | |
Chains B and R: 8 helices, 32 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-10 | 3 | |
| β-strand | 12 | 1 | 17 |
| β-strand | 17-19 | 3 | 18 |
| β-strand | 21 | 1 | 19 |
| β-strand | 28-30 | 3 | 18 |
| β-strand | 38 | 1 | 20 |
| β-strand | 46 | 1 | 21 |
| β-strand | 47 | 1 | 20 |
| β-strand | 49-56 | 8 | 21 |
| β-strand | 62-70 | 9 | 21 |
| β-strand | 75-79 | 5 | 21 |
| β-strand | 84-86 | 3 | 19 |
| β-strand | 92-104 | 13 | 21 |
| β-strand | 108-116 | 9 | 19 |
| β-strand | 122-131 | 10 | 19 |
| β-strand | 139 | 1 | 22 |
| β-strand | 149-156 | 8 | 23 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-177 | 3 | 24 |
| β-strand | 181-183 | 3 | 25 |
| β-strand | 188-190 | 3 | 25 |
| β-strand | 197-200 | 4 | 24 |
| β-strand | 208-211 | 4 | 24 |
| β-strand | 227-229 | 3 | 24 |
| β-strand | 235 | 1 | 17 |
| β-strand | 260-267 | 8 | 23 |
| α-helix | 270-273 | 4 | |
| β-strand | 274-277 | 4 | 26 |
| β-strand | 281-286 | 6 | 26 |
| β-strand | 292-298 | 7 | 22 |
| β-strand | 307-310 | 4 | 22 |
| β-strand | 314-319 | 6 | 26 |
| β-strand | 325-329 | 5 | 22 |
| α-helix | 333-334 | 2 | |
| β-strand | 335-337 | 3 | 22 |
| β-strand | 338-339 | 2 | 16 |
| α-helix | 351-360 | 10 | |
| α-helix | 365-396 | 32 | |
| α-helix | 398-400 | 3 | |
| α-helix | 408-413 | 6 | |
Chains c and N: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9 | 1 | 31 |
| β-strand | 16 | 1 | 31 |
| α-helix | 27-30 | 4 | |
| α-helix | 32-40 | 9 | |
| α-helix | 48-54 | 7 | |
Chain C: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 112-114 | 3 | |
| β-strand | 117-119 | 3 | 28 |
| β-strand | 127-129 | 3 | 28 |
| α-helix | 130-132 | 3 | |
| β-strand | 158-160 | 3 | 29 |
| β-strand | 166-168 | 3 | 29 |
| α-helix | 169-171 | 3 | |
| α-helix | 183-185 | 3 | |
| β-strand | 197-199 | 3 | 30 |
| β-strand | 205-207 | 3 | 30 |
| α-helix | 208-210 | 3 | |
Chains d and O: 4 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 108-118 | 11 | |
| β-strand | 120-125 | 6 | 34 |
| β-strand | 128-136 | 9 | 34 |
| β-strand | 139-142 | 4 | 34 |
| β-strand | 149-150 | 2 | 34 |
| α-helix | 153-157 | 5 | |
| β-strand | 161-163 | 3 | 34 |
| β-strand | 168-172 | 5 | 34 |
| α-helix | 173-174 | 2 | |
| α-helix | 175-180 | 6 | |
| β-strand | 182 | 1 | 34 |
| β-strand | 184 | 1 | 35 |
| β-strand | 191-195 | 5 | 35 |
| β-strand | 198-203 | 6 | 35 |
| β-strand | 206-209 | 4 | 35 |
| β-strand | 222-224 | 3 | 35 |
| β-strand | 230-240 | 11 | 35 |
| β-strand | 243-251 | 9 | 35 |
| β-strand | 256-259 | 4 | 35 |
| β-strand | 265-266 | 2 | 35 |
Chains D and T: 5 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 108-119 | 12 | |
| β-strand | 120-125 | 6 | 32 |
| β-strand | 128-136 | 9 | 32 |
| β-strand | 139-143 | 5 | 32 |
| β-strand | 149-150 | 2 | 32 |
| α-helix | 153-156 | 4 | |
| α-helix | 160 | 1 | |
| β-strand | 161-163 | 3 | 32 |
| β-strand | 168-172 | 5 | 32 |
| α-helix | 173-174 | 2 | |
| α-helix | 175-177 | 3 | |
| β-strand | 182 | 1 | 32 |
| β-strand | 184 | 1 | 33 |
| β-strand | 191-195 | 5 | 33 |
| β-strand | 198-203 | 6 | 33 |
| β-strand | 206-209 | 4 | 33 |
| β-strand | 222-224 | 3 | 33 |
| β-strand | 230-240 | 11 | 33 |
| β-strand | 243-251 | 9 | 33 |
| β-strand | 256-259 | 4 | 33 |
| β-strand | 265-266 | 2 | 33 |
9 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Spike glycoprotein E1 | A, E, F, G, H, U, V, W | protein | 438 | Semliki Forest virus 4 | P03315 (AlphaFold model) |
| Spike glycoprotein E2 | B, I, J, K, R, X, Y, Z | protein | 418 | Semliki Forest virus 4 | P03315 (AlphaFold model) |
| Very low-density lipoprotein receptor | C | protein | 121 | Homo sapiens | P98155 (AlphaFold model) |
| capsid protein, partial | D, O, P, Q, T, d, e, f | protein | 161 | Semliki Forest virus 4 | P03315 (AlphaFold model) |
| Spike glycoprotein E3 | L, M, N, S, a, b, c, g | protein | 52 | Semliki Forest virus 4 | P03315 (AlphaFold model) |
Sequence of entity 1 (A, E, F, G, H, U, V, W), FASTA
>8YW1_1 Spike glycoprotein E1 (chains A, E, F, G, H, U, V, W)
YEHSTVMPNVVGFPYKAHIERPGYSPLTLQMQVVETSLEPTLNLEYITCEYKTVVPSPYV
KCCGASECSTKEKPDYQCKVYTGVYPFMWGGAYCFCDSENTQLSEAYVDRSDVCRHDHAS
AYKAHTASLKAKVRVMYGNVNQTVDVYVNGDHAVTIGGTQFIFGPLSSAWTPFDNKIVVY
KDEVFNQDFPPYGSGQPGRFGDIQSRTVESNDLYANTALKLARPSPGMVHVPYTQTPSGF
KYWLKEKGTALNTKAPFGCQIKTNPVRAMNCAVGNIPVSMNLPDSAFTRIVEAPTIIDLT
CTVATCTHSSDFGGVLTLTYKTDKNGDCSVHSHSNVATLQEATAKVKTAGKVTLHFSTAS
ASPSFVVSLCSARATCSASCEPPKDHIVPYAASHSNVVFPDMSGTALSWVQKISGGLGAF
AIGAILVLVVVTCIGLRR
Sequence of entity 2 (B, I, J, K, R, X, Y, Z), FASTA
>8YW1_2 Spike glycoprotein E2 (chains B, I, J, K, R, X, Y, Z)
HFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDY
TKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRA
CRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAKTVEEIDMHMPPDTPDRTLLSQQ
SGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPR
ADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQ
YHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPA
ATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHA
Sequence of entity 3 (C), FASTA
>8YW1_3 Very low-density lipoprotein receptor (chains C)
RTCRIHEISCGAHSTQCIPVSWRCDGENDCDSGEDEENCGNITCSPDEFTCSSGRCISRN
FVCNGQDDCSDGSDELDCAPPTCGAHEFQCSTSSCIPISWVCDDDADCSDQSDESLEQCG
R
Sequence of entity 4 (D, O, P, Q, T, d, e, f), FASTA
>8YW1_4 capsid protein, partial (chains D, O, P, Q, T, d, e, f)
KRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKY
DLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDN
KGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEW
Sequence of entity 5 (L, M, N, S, a, b, c, g), FASTA
>8YW1_5 Spike glycoprotein E3 (chains L, M, N, S, a, b, c, g)
MCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCR
Primary citation
Structural insights into Semiliki forest virus receptor binding modes indicate novel mechanism of virus endocytosis. Yang, D., Wang, N., Du, B. et al. PLoS Pathog (2024) 20:e1012770-e1012770. DOI 10.1371/journal.ppat.1012770 · PubMed
Other PDB entries of the same protein (UniProt P03315 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2V33 1.55 Å, High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki…
- 1I9W 3.0 Å, Crystal structure of the fusion glycoprotein E1 from semliki forest virus
- 1VCP 3.0 Å, Semliki forest virus capsid protein (crystal form I)
- 2ALA 3.0 Å, Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric…
- 8IHP 3.0 Å, Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3
- 8YVY 3.02 Å, Semliki Forest virus virion
- 1VCQ 3.1 Å, Semliki forest virus capsid protein (crystal form II)
- 1RER 3.2 Å, Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.
- 8YVZ 3.45 Å, Semliki Forest virus viron
- 8X0K 3.5 Å, Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold)
- 8X0L 3.5 Å, Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold)
- 8X0M 3.5 Å, Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold)
Browse structure collections
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