Structure of PDB 1t3a Chain A Binding Site BS01

Receptor Information

>1t3a Chain A (length=400) Species: 1491 (Clostridium botulinum)

PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTT
PQDFHPPTSLKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGG
ILLEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIM
GAEPDLFETNSSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNSMNE
FIQDPALTLMHELIHSLHGLYGAKGITTKYTITGTNIEEFLTFGGTDLNI
ITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKDVFEAKYGLDKD
ASGIYSVNINKFNDIFKKLYSFTEFDLATKFQVKCRQTYIGQYKYFKLSN
LLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITGRGLVKKIIRFC

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 1t3a Chain A Residue 422

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1t3a 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
• Resolution: 2.16 Å
• Binding residue (original residue number in PDB): H211 H215 E250
• Binding residue (residue number reindexed from 1): H211 H215 E239
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): H211 E212 H215 E250 R347
• Catalytic site (residue number reindexed from 1): H211 E212 H215 E239 R336
• Enzyme Commision number: 3.4.24.69: bontoxilysin.

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity
• GO:0008270 zinc ion binding

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:1t3a, PDBe:1t3a, PDBj:1t3a
• PDBsum: 1t3a
• PubMed: 15157097
• UniProt: Q00496|BXE_CLOBO Botulinum neurotoxin type E (Gene Name=botE)