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PDBsum entry 2xhl

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
2xhl

 

 

 

 

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Contents
Protein chains
430 a.a. *
410 a.a. *
Metals
_ZN
Waters ×31
* Residue conservation analysis
PDB id:
2xhl
Name: Hydrolase
Title: Structure of a functional derivative of clostridium botulinum neurotoxin type b
Structure: Botulinum neurotoxin b light chain. Chain: a. Fragment: residues 1-437. Synonym: bont/b, bontoxilysin-b. Engineered: yes. Botulinum neurotoxin b heavy chain. Chain: b. Fragment: residues 446-858. Synonym: bont/b, bontoxilysin-b.
Source: Clostridium botulinum. Organism_taxid: 1491. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.80Å     R-factor:   0.242     R-free:   0.282
Authors: G.Masuyer,M.Beard,V.A.Cadd,J.A.Chaddock,K.R.Acharya
Key ref: G.Masuyer et al. (2011). Structure and activity of a functional derivative of Clostridium botulinum neurotoxin B. J Struct Biol, 174, 52-57. PubMed id: 21078393
Date:
18-Jun-10     Release date:   01-Dec-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P10844  (BXB_CLOBO) -  Botulinum neurotoxin type B from Clostridium botulinum
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1291 a.a.
430 a.a.*
Protein chain
Pfam   ArchSchema ?
P10844  (BXB_CLOBO) -  Botulinum neurotoxin type B from Clostridium botulinum
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1291 a.a.
410 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.3.4.24.69  - bontoxilysin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
      Cofactor: Zn(2+)

 

 
J Struct Biol 174:52-57 (2011)
PubMed id: 21078393  
 
 
Structure and activity of a functional derivative of Clostridium botulinum neurotoxin B.
G.Masuyer, M.Beard, V.A.Cadd, J.A.Chaddock, K.R.Acharya.
 
  ABSTRACT  
 
No abstract given.

 

 

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