eF-site ID 6ilm-ABCDEF
PDB Code 6ilm
Chain A, B, C, D, E, F

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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
B:  SDRVRSITLGNSTITTQESANVVVGYGVWPDYLSDEEATA
EDQPTQPDVATCRFYTLDSVSWMKESQGWWWKFPDALRDM
GLFGQNMQYHYLGRSGYTIHVQCNASKFHQGCLLVVCVPE
AEMGAANINEKINREHLSNGEVANTFSGTKSSNTNDVQQA
VFNAGMGVAVGNLTIFPHQWINLRTNNCATIVMPYINSVP
MDNMFRHYNFTLMIIPFAKLDYAAGSSTYIPITVTVAPMC
AEYNGLRLAGHQ
C:  GLPVMNTPGSNQFLTSDDYQSPTAMPQFDVTPEMNIPGEV
KNLMEIAEVDSVVPVNNVNENVNSLEAYRIPVHSVTETGA
QVFGFTLQPGADTVMERTLLGEILNYYANWSGSIKLTFMY
CGSAMATGKFLLAYSPPGAGVPKNRREAMLGTHIIWDIGL
QSSCVLCVPWISQTHYRFVSKDIYTDAGFITCWYQTSIVV
PAEVQNQSVILCFVSACNDFSVRLLRDSPFVRQTAFYQ
D:  GAQVSTQKTGAHETSIIHYTNINYYKDAASNSANRQDFTQ
DPGKFTEPVKDIMVKSLPALN
E:  LSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGE
AEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGG
KGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQ
GTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLR
EHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFY
PPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKS
GDEHHYCCIVQHAGLAQPLRVEL
F:  IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLL
KNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
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

13) chain D
residue 64
type
sequence L
description binding site for residue NA D 101
source : AC3

14) chain E
residue 250-256
type prosite
sequence YCCIVQH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YCCIVQH
source prosite : PS00290

15) chain F
residue 78-84
type prosite
sequence YACRVNH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YCCIVQH
source prosite : PS00290

16) chain F
residue 2
type MOD_RES
sequence Q
description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
source Swiss-Prot : SWS_FT_FI1

17) chain F
residue 1
type CARBOHYD
sequence I
description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI2

18) chain F
residue 19
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

19) chain F
residue 41
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

20) chain F
residue 48
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

21) chain F
residue 58
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

22) chain F
residue 91
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3

23) chain F
residue 94
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
source Swiss-Prot : SWS_FT_FI3


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