eF-site ID 4qd2-ABCDEFGHIJ
PDB Code 4qd2
Chain A, B, C, D, E, F, G, H, I, J

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Title Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex
Classification CELL ADHESION
Compound Hemagglutinin component HA33
Source Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) (CADH1_MOUSE)
Sequence A:  ENIQEINTAISDNYTYNINNPFYILFTVNTTGIYKINAQN
NLPSLKIYEAIGINYITGFDSPNAKSYLVVLLNKDKNYYI
RVPQTSSNIENQIQFKREEGDLRNLMNSSVNIIDNLNSTG
AHYYTRQSPDVHDYISYEFTIPGNFNNKDTSNIRLYTSYN
QGIGTLFRVTETIDGYNLINIQQNLHLLNNTNSIRLLNGA
IYILKVEVTELNNYNIRLHIDITN
B:  ERTFLPNGNYNIKSIFSGSLYLNPVSKSLTFSNESSANNQ
KWNVEYMAENRCFKISNVAEPNKYLSYDNFGFISLDSLSN
RCYWFPIKIAVNTYIMLSLNKVNELDYAWDIYDTNENILS
QPLLLLPNFDIYNSNQMFKLEKI
C:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW
RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS
NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK
LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ
QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL
SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE
TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW
NIRNPP
D:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW
RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS
NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK
LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ
QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL
SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE
TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW
NIRNPP
E:  WVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQ
GADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAV
SSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGA
VPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKN
MFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGL
STTAKAVITVKD
F:  ENIQEINTAISDNYTYNINNNPFYILFTVNTTGIYKINAQ
NNLPSLKIYEAIGINYITGFDSPNAKSYLVVLLNKDKNYY
IRVPQTSSNIENQIQFKREEGDLRNLMNSSVNIIDNLNST
GAHYYTRQSPDVHDYISYEFTIPGNFNNKDTSNIRLYTSY
NQGIGTLFRVTETIDGYNLINIQQNLHLLNNTNSIRLLNG
AIYILKVEVTELNNYNIRLHIDITN
G:  ERTFLPNGNYNIKSIFSGSLYLNPVSKSLTFSNESSANNQ
KWNVEYMAENRCFKISNVAEPNKYLSYDNFGFISLDSLSN
RCYWFPIKIAVNTYIMLSLNKVNELDYAWDIYDTNENILS
QPLLLLPNFDIYNSNQMFKLEKI
H:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW
RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS
NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK
LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ
QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL
SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE
TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW
NIRNPP
I:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW
RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS
NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK
LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ
QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL
SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE
TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW
NIRNPP
J:  WVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQ
GADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAV
SSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGA
VPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKN
MFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGL
STTAKAVITVKD
Description


Functional site

1) chain E
residue 11
type
sequence E
description BINDING SITE FOR RESIDUE CA E 301
source : AC1

2) chain E
residue 67
type
sequence D
description BINDING SITE FOR RESIDUE CA E 301
source : AC1

3) chain E
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE CA E 301
source : AC1

4) chain E
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE CA E 301
source : AC1

5) chain E
residue 11
type
sequence E
description BINDING SITE FOR RESIDUE CA E 302
source : AC2

6) chain E
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE CA E 302
source : AC2

7) chain E
residue 100
type
sequence D
description BINDING SITE FOR RESIDUE CA E 302
source : AC2

8) chain E
residue 101
type
sequence Q
description BINDING SITE FOR RESIDUE CA E 302
source : AC2

9) chain E
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE CA E 302
source : AC2

10) chain E
residue 136
type
sequence D
description BINDING SITE FOR RESIDUE CA E 302
source : AC2

11) chain E
residue 102
type
sequence N
description BINDING SITE FOR RESIDUE CA E 303
source : AC3

12) chain E
residue 104
type
sequence N
description BINDING SITE FOR RESIDUE CA E 303
source : AC3

13) chain E
residue 134
type
sequence D
description BINDING SITE FOR RESIDUE CA E 303
source : AC3

14) chain E
residue 136
type
sequence D
description BINDING SITE FOR RESIDUE CA E 303
source : AC3

15) chain E
residue 143
type
sequence N
description BINDING SITE FOR RESIDUE CA E 303
source : AC3

16) chain E
residue 195
type
sequence D
description BINDING SITE FOR RESIDUE CA E 303
source : AC3

17) chain J
residue 11
type
sequence E
description BINDING SITE FOR RESIDUE CA J 301
source : AC4

18) chain J
residue 67
type
sequence D
description BINDING SITE FOR RESIDUE CA J 301
source : AC4

19) chain J
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE CA J 301
source : AC4

20) chain J
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE CA J 301
source : AC4

21) chain J
residue 11
type
sequence E
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

22) chain J
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

23) chain J
residue 100
type
sequence D
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

24) chain J
residue 101
type
sequence Q
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

25) chain J
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

26) chain J
residue 104
type
sequence N
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

27) chain J
residue 136
type
sequence D
description BINDING SITE FOR RESIDUE CA J 302
source : AC5

28) chain J
residue 102
type
sequence N
description BINDING SITE FOR RESIDUE CA J 303
source : AC6

29) chain J
residue 104
type
sequence N
description BINDING SITE FOR RESIDUE CA J 303
source : AC6

30) chain J
residue 134
type
sequence D
description BINDING SITE FOR RESIDUE CA J 303
source : AC6

31) chain J
residue 136
type
sequence D
description BINDING SITE FOR RESIDUE CA J 303
source : AC6

32) chain J
residue 143
type
sequence N
description BINDING SITE FOR RESIDUE CA J 303
source : AC6

33) chain J
residue 195
type
sequence D
description BINDING SITE FOR RESIDUE CA J 303
source : AC6

34) chain E
residue 96-106
type prosite
sequence ITVTDQNDNRP
description CADHERIN_1 Cadherin domain signature. ItVtDqNDNrP
source prosite : PS00232

35) chain E
residue 103
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

36) chain E
residue 134
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

37) chain J
residue 103
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

38) chain J
residue 134
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI1

39) chain E
residue 126
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:28973932
source Swiss-Prot : SWS_FT_FI2

40) chain E
residue 131
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:28973932
source Swiss-Prot : SWS_FT_FI2

41) chain J
residue 126
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:28973932
source Swiss-Prot : SWS_FT_FI2

42) chain J
residue 131
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:28973932
source Swiss-Prot : SWS_FT_FI2

43) chain E
residue 204
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:28973932
source Swiss-Prot : SWS_FT_FI3

44) chain J
residue 204
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:28973932
source Swiss-Prot : SWS_FT_FI3


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