Structure of PDB 5v8p Chain B

Receptor sequence
>5v8pB (length=402) Species: 1491 (Clostridium botulinum) [Search protein sequence]
SSGLVPRGSHMQFVNKQFNYKDPVNGVDIAYIKIPQMQPVKAFKIHNKIW
VIPERDTFTNPEEGDLNPPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYS
TDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELN
LVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESL
EVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFEVSFEEL
RTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTASLQYMK
NVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRK
TYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFT
KL
3D structure
PDB5v8p Small molecule metalloprotease inhibitor with in vitro, ex vivo and in vivo efficacy against botulinum neurotoxin serotype A.
ChainB
Resolution2.501 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) H223 E224 H227 E249 R349
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 90G B V70 I161 F163 F194 H223 E224 H227 E262 Y366 F369 V70 I161 F163 F194 H223 E224 H227 E249 Y352 F355 MOAD: Ki=10.2uM
BS02 ZN B H223 H227 E262 H223 H227 E249
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:5v8p, PDBe:5v8p, PDBj:5v8p
PDBsum5v8p
PubMed28698055
UniProtP0DPI1|BXA1_CLOBH Botulinum neurotoxin type A (Gene Name=botA)

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