eF-site ID 3ffz-AB
PDB Code 3ffz
Chain A, B

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Title Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation
Classification HYDROLASE
Compound Botulinum neurotoxin type E
Source ORGANISM_SCIENTIFIC: Clostridium botulinum;
Sequence A:  PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWI
IPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKD
RFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPD
NQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETN
SSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNCMNE
FIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLI
TNIRGTNIEEFLTFGGTDLNIITSAQSNDIYTNLLADYKK
IASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNI
NKFNDIFKKLYSFTEFDLATKFQVKCRQTYIGQYKYFKLS
NLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITG
RGLVKKIIRFCKNIVSVKGIRKSICIEINNGELFFVASEN
SYNDDNINTPKEIDDTVTSNDLDQVILNFNSESAPGLSDE
KLNLTIQNDAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQ
KVPEGENNVNLTSSIDTALLEQPKIYTFFSSEFINNVNKP
VQAALFVSWIQQVLVDFTTEANQKSTVDKIADISIVVPYI
GLALNIGNEAQKGNFKDALELLGAGILLEFEPELLIPTIL
VFTIKSFLGSSDNKNKVIKAINNALKERDEKWKEVYSFIV
SNWMTKINTQFNKRKEQMYQALQNQVNAIKTIIESKYNSY
TLEEKNELTNKYDIKQIENELNQKVSIAMNNIDRFLTESS
ISYLMKIINEVKINKLREYDENVKTYLLNYIIQHGSILGE
SQQELNSMVTDTLNNSIPFKLSSYTDDKILISYFNKFFKR
IKSSSVLNMRYKNDKYVDTSGYDSNININGDVYKYPTNKN
QFGIYNDKLSEVNISQNDYIIYDNKYKNFSISFWVRIPNY
DNKIVNVNNEYTIINCMRDNNSGWKVSLNHNEIIWTLQDN
AGINQKLAFNYGNANGISDYINKWIFVTITNDRLGDSKLY
INGNLIDQKSILNLGNIHVSDNILFKIVNCSYTRYIGIRY
FNIFDKELDETEIQTLYSNEPNTNILKDFWGNYLLYDKEY
YLLNVLKPNNFIDRRKDSTLSINNIRSTILLANRLYSGIK
VKIQRVNNSSTNDNLVRKNDQVYINFVASKTHLFPLYADT
ATTNKEKTIKISSSGNRFNQVVVMNSVGNNCTMNFKNNNG
NNIGLLGFKADTVVASTWYYTHMRDHTNSNGCFWNFISEE
HGWQEK
B:  PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWI
IPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKD
RFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPD
NQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETN
SSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNCMNE
FIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLI
TNIRGTNIEEFLTFGGTDLNIITSAQSNDIYTNLLADYKK
IASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNI
NKFNDIFKKLYSFTEFDLATKFQVKCRQTYIGQYKYFKLS
NLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITG
RGLVKKIIRFCKNKSICIEINNGELFFVASENSYNDDNIN
TPKEIDDTVTSNDLDQVILNFNSESAPGLSDEKLNLTIQN
DAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQKVPEGENN
VNLTSSIDTALLEQPKIYTFFSSEFINNVNKPVQAALFVS
WIQQVLVDFTTEANQKSTVDKIADISIVVPYIGLALNIGN
EAQKGNFKDALELLGAGILLEFEPELLIPTILVFTIKSFL
GSSDNKNKVIKAINNALKERDEKWKEVYSFIVSNWMTKIN
TQFNKRKEQMYQALQNQVNAIKTIIESKYNSYTLEEKNEL
TNKYDIKQIENELNQKVSIAMNNIDRFLTESSISYLMKII
NEVKINKLREYDENVKTYLLNYIIQHGSILGESQQELNSM
VTDTLNNSIPFKLSSYTDDKILISYFNKFFKRIKSSSVLN
MRYKNDKYVDTSGYDSNININGDVYKYPTNKNQFGIYNDK
LSEVNISQNDYIIYDNKYKNFSISFWVRIPNYDNKIVNVN
NEYTIINCMRDNNSGWKVSLNHNEIIWTLQDNAGINQKLA
FNYGNANGISDYINKWIFVTITNDRLGDSKLYINGNLIDQ
KSILNLGNIHVSDNILFKIVNCSYTRYIGIRYFNIFDKEL
DETEIQTLYSNEPNTNILKDFWGNYLLYDKEYYLLNVLKP
NNFIDRRKDSTLSINNIRSTILLANRLYSGIKVKIQRVNN
SSTNDNLVRKNDQVYINFVASKTHLFPLYADTATTNKEKT
IKISSSGNRFNQVVVMNSVGNNCTMNFKNNNGNNIGLLGF
KADTVVASTWYYTHMRDHTNSNGCFWNFISEEHGWQEK
Description


Functional site

1) chain A
residue 212
type
sequence H
description BINDING SITE FOR RESIDUE ZN A1300
source : AC1

2) chain A
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE ZN A1300
source : AC1

3) chain A
residue 251
type
sequence E
description BINDING SITE FOR RESIDUE ZN A1300
source : AC1

4) chain A
residue 544
type
sequence A
description BINDING SITE FOR RESIDUE NA A1301
source : AC2

5) chain A
residue 547
type
sequence E
description BINDING SITE FOR RESIDUE NA A1301
source : AC2

6) chain A
residue 548
type
sequence Q
description BINDING SITE FOR RESIDUE NA A1301
source : AC2

7) chain A
residue 550
type
sequence K
description BINDING SITE FOR RESIDUE NA A1301
source : AC2

8) chain A
residue 593
type
sequence V
description BINDING SITE FOR RESIDUE NA A1302
source : AC3

9) chain A
residue 596
type
sequence I
description BINDING SITE FOR RESIDUE NA A1302
source : AC3

10) chain A
residue 597
type
sequence A
description BINDING SITE FOR RESIDUE NA A1302
source : AC3

11) chain A
residue 599
type
sequence I
description BINDING SITE FOR RESIDUE NA A1302
source : AC3

12) chain A
residue 879
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A1303
source : AC4

13) chain A
residue 1041
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A1303
source : AC4

14) chain B
residue 212
type
sequence H
description BINDING SITE FOR RESIDUE ZN B1300
source : AC5

15) chain B
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE ZN B1300
source : AC5

16) chain B
residue 251
type
sequence E
description BINDING SITE FOR RESIDUE ZN B1300
source : AC5

17) chain B
residue 593
type
sequence V
description BINDING SITE FOR RESIDUE NA B1302
source : AC6

18) chain B
residue 596
type
sequence I
description BINDING SITE FOR RESIDUE NA B1302
source : AC6

19) chain B
residue 599
type
sequence I
description BINDING SITE FOR RESIDUE NA B1302
source : AC6

20) chain B
residue 600
type
sequence S
description BINDING SITE FOR RESIDUE NA B1302
source : AC6

21) chain B
residue 879
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B1303
source : AC7

22) chain B
residue 881
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B1303
source : AC7

23) chain A
residue 209-218
type prosite
sequence TLMHELIHSL
description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLMHELIHSL
source prosite : PS00142

24) chain A
residue 213
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:15157097
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 213
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:15157097
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 212
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 216
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 212
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 216
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 251
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ
source Swiss-Prot : SWS_FT_FI3

31) chain B
residue 251
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ
source Swiss-Prot : SWS_FT_FI3


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