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eF-site ID
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3ffz-B |
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PDB Code
|
3ffz |
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Chain
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B |
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click to enlarge
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Title
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Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation |
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Classification
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HYDROLASE |
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Compound
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Botulinum neurotoxin type E |
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Source
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ORGANISM_SCIENTIFIC: Clostridium botulinum; |
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Sequence
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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
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Description
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Functional site
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|
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1)
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chain |
B |
| residue |
212 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN B1300
|
| source |
: AC5
|
|
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2)
|
chain |
B |
| residue |
216 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN B1300
|
| source |
: AC5
|
|
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3)
|
chain |
B |
| residue |
251 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ZN B1300
|
| source |
: AC5
|
|
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4)
|
chain |
B |
| residue |
593 |
| type |
|
| sequence |
V
|
| description |
BINDING SITE FOR RESIDUE NA B1302
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| source |
: AC6
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|
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5)
|
chain |
B |
| residue |
596 |
| type |
|
| sequence |
I
|
| description |
BINDING SITE FOR RESIDUE NA B1302
|
| source |
: AC6
|
|
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6)
|
chain |
B |
| residue |
599 |
| type |
|
| sequence |
I
|
| description |
BINDING SITE FOR RESIDUE NA B1302
|
| source |
: AC6
|
|
|
7)
|
chain |
B |
| residue |
600 |
| type |
|
| sequence |
S
|
| description |
BINDING SITE FOR RESIDUE NA B1302
|
| source |
: AC6
|
|
|
8)
|
chain |
B |
| residue |
879 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE ACT B1303
|
| source |
: AC7
|
|
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9)
|
chain |
B |
| residue |
881 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE ACT B1303
|
| source |
: AC7
|
|
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10)
|
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
|
|
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11)
|
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
|
|
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12)
|
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
|
|
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13)
|
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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