Structure of PDB 1e1h Chain C

Receptor sequence
>1e1hC (length=235) Species: 1491 (Clostridium botulinum) [Search protein sequence]
MAYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEG
DLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRML
LTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPS
ADIIQFECKSFGHDVLNLTRNGYGSTQYIRFSPDFTFGFEESLGAGKFAT
DPAVTLAHELIHAEHRLYGIAINPNRVFKVNTNAY
3D structure
PDB1e1h Crystal Structure of Clostridium Botulinum Neurotoxin Protease in a Product-Bound State: Evidence for Noncanonical Zinc Protease Activity
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 C H222 H226 H208 H212
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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