Structure of PDB 4ktx Chain A

Receptor sequence
>4ktxA (length=428) Species: 441771 (Clostridium botulinum A str. Hall) [Search protein sequence]
GSHMPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPE
RDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFER
IYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNSINVIQPDGSYRSE
ELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFE
ESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNT
NAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTL
NKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTE
IYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNL
AANFNGQNTEINNMNFTKLKNFTGLFEF
3D structure
PDB4ktx Covalent modification of the active site cysteine stresses Clostridium botulinum neurotoxin A
ChainA
Resolution2.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H223 E224 H227 E262 R363
Catalytic site (residue number reindexed from 1) H226 E227 H230 E265 R366
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 peptide A Q162 F163 E164 C165 F194 H223 E224 H227 E262 R363 Y366 D370 Q165 F166 E167 C168 F197 H226 E227 H230 E265 R366 Y369 D373
BS02 ZN A H223 H227 E262 N368 H226 H230 E265 N371
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:4ktx, PDBe:4ktx, PDBj:4ktx
PDBsum4ktx
PubMed
UniProtP0DPI1|BXA1_CLOBH Botulinum neurotoxin type A (Gene Name=botA)

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