Structure of PDB 1zkw Chain A

Receptor sequence
>1zkwA (length=411) Species: 1491 (Clostridium botulinum) [Search protein sequence]
PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTT
PQDFHPPTSLKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGG
ILLEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIM
GAEPDLFETNSSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNSMNE
FIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLITNIRGTNIEE
FLTFGGTDLNIITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKD
VFEAKYGLDKDASGIYSVNINKFNDIFKKLYSFTEFDLATKFQVKCAQTY
IGQYKYFKLSNLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITG
RGLVKKIIRFC
3D structure
PDB1zkw Analysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme.
ChainA
Resolution2.17 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H211 E212 H215 E250 A347
Catalytic site (residue number reindexed from 1) H211 E212 H215 E250 A347
Enzyme Commision number 3.4.24.69: bontoxilysin.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN A H211 H215 E250 H211 H215 E250
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1zkw, PDBe:1zkw, PDBj:1zkw
PDBsum1zkw
PubMed15938619
UniProtQ00496|BXE_CLOBO Botulinum neurotoxin type E (Gene Name=botE)

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