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