Structure of PDB 4hev Chain A

Receptor sequence
>4hevA (length=397) Species: 1491 (Clostridium botulinum) [Search protein sequence]
SSGLVPRGSHMQFVNKQFNYKDPVNGVDIAYIKIPQMQPVKAFKIHNKIW
VIPERDTFTNPEEGDLNPPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYS
TDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELN
LVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESL
ELGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVEVSFEELRTFGGHD
AKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEK
YLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFD
KAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLK
3D structure
PDB4hev Evaluation of adamantane hydroxamates as botulinum neurotoxin inhibitors: synthesis, crystallography, modeling, kinetic and cellular based studies.
ChainA
Resolution2.5 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) H217 E218 H221 E242 R343
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 H223 H227 E262 H217 H221 E242
BS02 AXM A F163 F194 E224 H227 E262 Y366 F163 F194 E218 H221 E242 Y346 MOAD: Ki=460nM
PDBbind-CN: -logKd/Ki=6.34,Ki=0.46uM
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:4hev, PDBe:4hev, PDBj:4hev
PDBsum4hev
PubMed23340139
UniProtP0DPI1|BXA1_CLOBH Botulinum neurotoxin type A (Gene Name=botA)

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