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BioLiP

Structure of PDB 1e1h Chain C Binding Site BS01

Receptor Information
>1e1h Chain C (length=235) Species: 1491 (Clostridium botulinum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MAYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEG
DLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRML
LTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPS
ADIIQFECKSFGHDVLNLTRNGYGSTQYIRFSPDFTFGFEESLGAGKFAT
DPAVTLAHELIHAEHRLYGIAINPNRVFKVNTNAY
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1e1h Chain C Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1e1h Crystal Structure of Clostridium Botulinum Neurotoxin Protease in a Product-Bound State: Evidence for Noncanonical Zinc Protease Activity
Resolution1.8 Å
Binding residue
(original residue number in PDB)		H222 H226
Binding residue
(residue number reindexed from 1)		H208 H212
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S70 R144 H222 E223 H226 A248
Catalytic site (residue number reindexed from 1) S64 R138 H208 E209 H212 A234
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1e1h, PDBe:1e1h, PDBj:1e1h
PDBsum1e1h
PubMed15107500
UniProtQ45894|BXA2_CLOBJ Botulinum neurotoxin type A2 (Gene Name=botA)

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