Structure of PDB 1t3c Chain A

Receptor sequence
>1t3cA (length=411) Species: 1491 (Clostridium botulinum) [Search protein sequence]
PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTT
PQDFHPPTSLKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGG
ILLEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIM
GAEPDLFETNSSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNSMNE
FIQDPALTLMHQLIHSLHGLYGAKGITTKYTITQKQNPLITNIRGTNIEE
FLTFGGTDLNIITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKD
VFEAKYGLDKDASGIYSVNINKFNDIFKKLYSFTEFDLATKFQVKCRQTY
IGQYKYFKLSNLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITG
RGLVKKIIRFC
3D structure
PDB1t3c Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway
ChainA
Resolution1.9 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 Q212 H215 E250 R347
Catalytic site (residue number reindexed from 1) H211 Q212 H215 E250 R347
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1t3c, PDBe:1t3c, PDBj:1t3c
PDBsum1t3c
PubMed15157097
UniProtQ00496|BXE_CLOBO Botulinum neurotoxin type E (Gene Name=botE)

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