Structure of PDB 3boo Chain A Binding Site BS01

Receptor Information
>3boo Chain A (length=419) Species: 1491 (Clostridium botulinum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDT
FTNPEEGDLNPVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRM
LLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGP
SADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNP
LLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGL
EVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGT
TASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVK
FFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNT
EINNMNFTKLKNFTGLFEF
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3boo Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex.
Resolution1.4 Å
Binding residue
(original residue number in PDB)		V70 I161 F163 F194 H223 E224 H227 E262 R363 Y366 D370
Binding residue
(residue number reindexed from 1)		V64 I155 F157 F188 H217 E218 H221 E256 R357 Y360 D364
Enzymatic activity
Catalytic site (original residue number in PDB) H223 E224 H227 E262 R363
Catalytic site (residue number reindexed from 1) H217 E218 H221 E256 R357
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3boo, PDBe:3boo, PDBj:3boo
PDBsum3boo
PubMed18457419
UniProtP0DPI1|BXA1_CLOBH Botulinum neurotoxin type A (Gene Name=botA)

[Back to BioLiP]