6ILK: Echovirus 6
Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 7.4. Determined by electron microscopy at 3.0 Å resolution. Released 15 May 2019.
- Method
- Electron microscopy
- Resolution
- 3.0 Å
- Organisms
- Echovirus E6, Homo sapiens
- Chains
- 5
- Atoms
- 8,025
- Mol. weight
- 115.1 kDa
- Ligands
- SPH
- Released
- 15 May 2019
Explore 6ILK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6ILK contains 35 α-helices and 93 β-strands across 5 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.
Chain A: 10 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 13 | 1 | 1 |
| α-helix | 14-16 | 3 | |
| β-strand | 17 | 1 | 2 |
| α-helix | 18-19 | 2 | |
| β-strand | 32 | 1 | 3 |
| α-helix | 34-36 | 3 | |
| β-strand | 53 | 1 | 2 |
| β-strand | 58 | 1 | 1 |
| β-strand | 63 | 1 | 4 |
| α-helix | 64-68 | 5 | |
| β-strand | 75-80 | 6 | 5 |
| β-strand | 90-94 | 5 | 6 |
| α-helix | 101-107 | 7 | |
| β-strand | 110-127 | 18 | 5 |
| β-strand | 141-147 | 7 | 6 |
| α-helix | 160-162 | 3 | |
| β-strand | 169-173 | 5 | 6 |
| α-helix | 177-179 | 3 | |
| β-strand | 180-183 | 4 | 5 |
| β-strand | 192-193 | 2 | 5 |
| β-strand | 198 | 1 | 7 |
| β-strand | 199 | 1 | 8 |
| β-strand | 208 | 1 | 8 |
| α-helix | 210-213 | 4 | |
| β-strand | 218-223 | 6 | 6 |
| β-strand | 232-250 | 19 | 5 |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 9 |
| α-helix | 257-258 | 2 | |
| β-strand | 275 | 1 | 10 |
Chain B: 9 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 14-18 | 5 | 11 |
| β-strand | 21-25 | 5 | 11 |
| β-strand | 32 | 1 | 12 |
| α-helix | 37-39 | 3 | |
| α-helix | 41-43 | 3 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54 | 1 | 13 |
| β-strand | 64-65 | 2 | 13 |
| β-strand | 69-70 | 2 | 13 |
| β-strand | 78-81 | 4 | 14 |
| α-helix | 82-85 | 4 | |
| α-helix | 90-98 | 9 | |
| β-strand | 99-112 | 14 | 13 |
| β-strand | 119-128 | 10 | 14 |
| α-helix | 132-133 | 2 | |
| β-strand | 134 | 1 | 15 |
| α-helix | 143-146 | 4 | |
| β-strand | 148 | 1 | 16 |
| β-strand | 151 | 1 | 16 |
| α-helix | 152 | 1 | |
| β-strand | 153-154 | 2 | 14 |
| β-strand | 166 | 1 | 15 |
| β-strand | 177 | 1 | 9 |
| α-helix | 179-184 | 6 | |
| β-strand | 187-191 | 5 | 14 |
| β-strand | 198-202 | 5 | 13 |
| β-strand | 211 | 1 | 13 |
| β-strand | 216 | 1 | 7 |
| β-strand | 219-230 | 12 | 14 |
| β-strand | 233 | 1 | 17 |
| β-strand | 235 | 1 | 17 |
| β-strand | 240-255 | 16 | 13 |
Chain C: 7 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 23 | 1 | 5 |
| α-helix | 30-33 | 4 | |
| β-strand | 39-40 | 2 | 5 |
| β-strand | 42 | 1 | 4 |
| α-helix | 44-47 | 4 | |
| β-strand | 51-52 | 2 | 3 |
| β-strand | 58 | 1 | 10 |
| α-helix | 61-63 | 3 | |
| α-helix | 65-68 | 4 | |
| β-strand | 70-72 | 3 | 3 |
| β-strand | 83-86 | 4 | 18 |
| α-helix | 99-104 | 6 | |
| β-strand | 109-111 | 3 | 19 |
| β-strand | 114-121 | 8 | 3 |
| β-strand | 127 | 1 | 20 |
| β-strand | 129-135 | 7 | 18 |
| β-strand | 137 | 1 | 21 |
| β-strand | 139 | 1 | 21 |
| α-helix | 145-148 | 4 | |
| β-strand | 152-157 | 6 | 18 |
| β-strand | 163-168 | 6 | 3 |
| β-strand | 177-178 | 2 | 19 |
| β-strand | 189-194 | 6 | 18 |
| β-strand | 199 | 1 | 20 |
| β-strand | 208-216 | 9 | 3 |
| β-strand | 221-222 | 2 | 19 |
Chain D: 3 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 22 |
| α-helix | 7-8 | 2 | |
| β-strand | 25-28 | 4 | 22 |
| α-helix | 35-37 | 3 | |
| α-helix | 39-40 | 2 | |
| β-strand | 56 | 1 | 12 |
Chain E: 6 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 69-70 | 2 | |
| β-strand | 75-77 | 3 | 23 |
| β-strand | 92-94 | 3 | 24 |
| β-strand | 95-97 | 3 | 23 |
| β-strand | 101-103 | 3 | 25 |
| β-strand | 110-112 | 3 | 24 |
| β-strand | 113 | 1 | 26 |
| β-strand | 119 | 1 | 26 |
| α-helix | 120-121 | 2 | |
| β-strand | 126-128 | 3 | 25 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 27 |
| α-helix | 131-133 | 3 | |
| β-strand | 140-143 | 4 | 28 |
| β-strand | 149 | 1 | 27 |
| β-strand | 153-158 | 6 | 28 |
| β-strand | 162-165 | 4 | 29 |
| β-strand | 169-171 | 3 | 28 |
| β-strand | 172-175 | 4 | 30 |
| β-strand | 178-181 | 4 | 30 |
| β-strand | 187-190 | 4 | 29 |
| α-helix | 191 | 1 | |
| β-strand | 193 | 1 | 31 |
| α-helix | 195-199 | 5 | |
| β-strand | 204 | 1 | 32 |
| β-strand | 211 | 1 | 31 |
| β-strand | 216-218 | 3 | 33 |
| β-strand | 219 | 1 | 32 |
| β-strand | 227-228 | 2 | 34 |
| β-strand | 232-234 | 3 | 33 |
| β-strand | 235-238 | 4 | 35 |
| β-strand | 241-244 | 4 | 35 |
| β-strand | 250-251 | 2 | 34 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Capsid protein VP1 | A | protein | 278 | Echovirus E6 | |
| Capsid protein VP2 | B | protein | 252 | Echovirus E6 | |
| Capsid protein VP3 | C | protein | 238 | Echovirus E6 | |
| Capsid protein VP4 | D | protein | 68 | Echovirus E6 | |
| Complement decay-accelerating factor | E | protein | 192 | Homo sapiens | P08174 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>6ILK_1 Capsid protein VP1 (chains A)
VVRVADTMPSGPSNSESIPALTAAETGHTSQVVPSDTIQTRHVRNFHVRSESSVENFLSR
SACVYIVEYKTRDDTPDKMYDSWVINTRQVAQLRRKLEFFTYVRFDVEVTFVITSVQDDS
TRQNTDTPALTHQIMYVPPGGPIPQAVDDYNWQTSTNPSVFWTEGNAPPRMSIPFMSVGN
AYSNFYDGWSHFSQTGVYGFNTLNNMGKLYFRHVNDKTISPITSKVRIYFKPKHVKAWVP
RPPRLCEYTHKDNVDFEPKGVTTSRTQLTISNSTHVEN
Sequence of entity 2 (B), FASTA
>6ILK_2 Capsid protein VP2 (chains B)
SDRVRSITLGNSTITTQESANVVVGYGVWPDYLSDEEATAEDQPTQPDVATCRFYTLDSV
SWMKESQGWWWKFPDALRDMGLFGQNMQYHYLGRSGYTIHVQCNASKFHQGCLLVVCVPE
AEMGAANINEKINREHLSNGEVANTFSGTKSSNTNDVQQAVFNAGMGVAVGNLTIFPHQW
INLRTNNCATIVMPYINSVPMDNMFRHYNFTLMIIPFAKLDYAAGSSTYIPITVTVAPMC
AEYNGLRLAGHQ
Sequence of entity 3 (C), FASTA
>6ILK_3 Capsid protein VP3 (chains C)
GLPVMNTPGSNQFLTSDDYQSPTAMPQFDVTPEMNIPGEVKNLMEIAEVDSVVPVNNVNE
NVNSLEAYRIPVHSVTETGAQVFGFTLQPGADTVMERTLLGEILNYYANWSGSIKLTFMY
CGSAMATGKFLLAYSPPGAGVPKNRREAMLGTHIIWDIGLQSSCVLCVPWISQTHYRFVS
KDIYTDAGFITCWYQTSIVVPAEVQNQSVILCFVSACNDFSVRLLRDSPFVRQTAFYQ
Sequence of entity 4 (D), FASTA
>6ILK_4 Capsid protein VP4 (chains D)
GAQVSTQKTGAHETSLSASGNSIIHYTNINYYKDAASNSANRQDFTQDPGKFTEPVKDIM
VKSLPALN
Sequence of entity 5 (E), FASTA
>6ILK_5 Complement decay-accelerating factor (chains E)
CNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWST
AVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQW
SDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDE
GEWSGPPPECRG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| SPH | Sphingosine | C18 H37 N O2 | 1 |
Primary citation
Human Neonatal Fc Receptor Is the Cellular Uncoating Receptor for Enterovirus B. Zhao, X., Zhang, G., Liu, S. et al. Cell (2019) 177:1553-1565.e16. DOI 10.1016/j.cell.2019.04.035 · PubMed
Other PDB entries of the same protein (UniProt P08174 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1H03 1.7 Å, Human CD55 domains 3 & 4
- 1H04 2.0 Å, Human CD55 domains 3 & 4
- 1OK3 2.2 Å, Decay accelerating factor (cd55): the structure of an intact human complement regulator.
- 1OJV 2.3 Å, Decay accelerating factor (CD55): the structure of an intact human complement regulator.
- 1OJW 2.3 Å, Decay accelerating factor (CD55): the structure of an intact human complement regulator.
- 1OK2 2.5 Å, Decay accelerating factor (CD55): the structure of an intact human complement regulator.
- 1OJY 2.6 Å, Decay accelerating factor (cd55): the structure of an intact human complement regulator.
- 1OK1 2.6 Å, Decay accelerating factor (cd55) : the structure of an intact human complement regulator.
- 8K9T 2.66 Å, Cryo-EM structure of the products-bound PGAP1(Bst1)-S327A from Chaetonium thermophilum
- 8K9R 2.68 Å, Cryo EM structure of the products-bound PGAP1(Bst1)-H443N from Chaetomium thermophilum
- 1H2P 2.8 Å, Human CD55 domains 3 & 4
- 6LA5 2.86 Å, Cryo-EM structure of echovirus 11 complexed with its attaching receptor CD55 at pH 7.4
Browse structure collections
About this viewer
MolViewer shows 6ILK 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.