eF-site ID 6ilm-A
PDB Code 6ilm
Chain A

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Title Cryo-EM structure of Echovirus 6 complexed with its uncoating receptor FcRn at PH 7.4
Classification VIRUS
Compound Capsid protein VP1
Source ORGANISM_SCIENTIFIC: Echovirus E6;
Sequence A:  NDVQNAIDRAVVRVADTMPSGPSNSESIPALTAAETGHTS
QVVPSDTIQTRHVRNFHVRSESSVENFLSRSACVYIVEYK
TRDDTPDKMYDSWVINTRQVAQLRRKLEFFTYVRFDVEVT
FVITSVQDDSTRQNTDTPALTHQIMYVPPGGPIPQAVDDY
NWQTSTNPSVFWTEGNAPPRMSIPFMSVGNAYSNFYDGWS
HFSQTGVYGFNTLNNMGKLYFRHVNDKTISPITSKVRIYF
KPKHVKAWVPRPPRLCEYTHKDNVDFEPKGVTTSRTQLTI
SNSTHVENY
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), Capsid protein VP4 (E.C.3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48), FcRn heavy chain, FcRn light chain


Functional site

1) chain A
residue 97
type
sequence T
description binding site for residue SPH A 301
source : AC1

2) chain A
residue 115
type
sequence F
description binding site for residue SPH A 301
source : AC1

3) chain A
residue 146
type
sequence Y
description binding site for residue SPH A 301
source : AC1

4) chain A
residue 183
type
sequence I
description binding site for residue SPH A 301
source : AC1

5) chain A
residue 192
type
sequence Y
description binding site for residue SPH A 301
source : AC1

6) chain A
residue 194
type
sequence N
description binding site for residue SPH A 301
source : AC1

7) chain A
residue 216
type
sequence M
description binding site for residue SPH A 301
source : AC1

8) chain A
residue 219
type
sequence L
description binding site for residue SPH A 301
source : AC1

9) chain A
residue 14
type
sequence V
description binding site for residue K A 302
source : AC2

10) chain A
residue 16
type
sequence D
description binding site for residue K A 302
source : AC2

11) chain A
residue 55
type
sequence N
description binding site for residue K A 302
source : AC2

12) chain A
residue 31
type
sequence L
description binding site for residue NA D 101
source : AC3


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