|
|
eF-site ID
|
6ilj-ABCDE |
|
PDB Code
|
6ilj |
|
Chain
|
A, B, C, D, E |
|
click to enlarge
|
|
|
Title
|
Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 5.5 |
|
Classification
|
VIRUS |
|
Compound
|
Capsid protein VP1 |
|
Source
|
ORGANISM_SCIENTIFIC: Echovirus E6; |
|
|
Sequence
|
A: |
VVRVADTMPSGPSNSESIPALTAAETGHTSQVVPSDTIQT
RHVRNFHVRSESSVENFLSRSACVYIVEYKTRDDTPDKMY
DSWVINTRQVAQLRRKLEFFTYVRFDVEVTFVITSVQDDS
TRQNTDTPALTHQIMYVPPGGPIPQAVDDYNWQTSTNPSV
FWTEGNAPPRMSIPFMSVGNAYSNFYDGWSHFSQTGVYGF
NTLNNMGKLYFRHVNDKTISPITSKVRIYFKPKHVKAWVP
RPPRLCEYTHKDNVDFEPKGVTTSRTQLTISNSTHVEN
|
| B: |
SDRVRSITLGNSTITTQESANVVVGYGVWPDYLSDEEATA
EDQPTQPDVATCRFYTLDSVSWMKESQGWWWKFPDALRDM
GLFGQNMQYHYLGRSGYTIHVQCNASKFHQGCLLVVCVPE
AEMGAANINEKINREHLSNGEVANTFSGTKSSNTNDVQQA
VFNAGMGVAVGNLTIFPHQWINLRTNNCATIVMPYINSVP
MDNMFRHYNFTLMIIPFAKLDYAAGSSTYIPITVTVAPMC
AEYNGLRLAGHQ
|
| C: |
GLPVMNTPGSNQFLTSDDYQSPTAMPQFDVTPEMNIPGEV
KNLMEIAEVDSVVPVNNVNENVNSLEAYRIPVHSVTETGA
QVFGFTLQPGADTVMERTLLGEILNYYANWSGSIKLTFMY
CGSAMATGKFLLAYSPPGAGVPKNRREAMLGTHIIWDIGL
QSSCVLCVPWISQTHYRFVSKDIYTDAGFITCWYQTSIVV
PAEVQNQSVILCFVSACNDFSVRLLRDSPFVRQTAFYQ
|
| D: |
GAQVSTQKTGAHEIIHYTNINYYKDAASNSANRQDFTQDP
GKFTEPVKDIMVKSLPALN
|
| E: |
CNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGY
RREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQ
IDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQW
SDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYAC
NKGFTMIGEHSIYCTVNNDEGEWSGPPPECRG
|
|
|
Description
|
(1) |
Capsid protein VP1 (E.C.3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48), Capsid protein VP2 (E.C.3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48), Capsid protein VP3 (E.C.3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48), Genome polyprotein (E.C.3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48), Complement decay-accelerating factor
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
95 |
| type |
|
| sequence |
I
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
2)
|
chain |
A |
| residue |
97 |
| type |
|
| sequence |
T
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
3)
|
chain |
A |
| residue |
115 |
| type |
|
| sequence |
F
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
4)
|
chain |
A |
| residue |
146 |
| type |
|
| sequence |
Y
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
5)
|
chain |
A |
| residue |
168 |
| type |
|
| sequence |
P
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
6)
|
chain |
A |
| residue |
183 |
| type |
|
| sequence |
I
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
7)
|
chain |
A |
| residue |
192 |
| type |
|
| sequence |
Y
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
8)
|
chain |
A |
| residue |
194 |
| type |
|
| sequence |
N
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
9)
|
chain |
A |
| residue |
240 |
| type |
|
| sequence |
F
|
| description |
binding site for residue SPH A 301
|
| source |
: AC1
|
|
|
10)
|
chain |
E |
| residue |
63 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|