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PDBsum entry 2xrm

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protein ligands metals links
Hydrolase PDB id
2xrm

 

 

 

 

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Contents
Protein chain
301 a.a.
Ligands
1PE
Metals
_NA
_SR
_CA
Waters ×26
PDB id:
2xrm
Name: Hydrolase
Title: Processed intracellular subtilisin from b. Clausii
Structure: Intracellular subtilisin protease. Chain: a. Fragment: processed protein, residues 19-321. Engineered: yes. Mutation: yes. Other_details: n terminal 18 residues deleted
Source: Bacillus clausii. Organism_taxid: 79880. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Other_details: isolated from a novozymes strain b. Clausii strain - strain number available on request.
Resolution:
2.60Å     R-factor:   0.202     R-free:   0.281
Authors: M.Gamble,G.Kunze,E.J.Dodson,D.D.Jones,K.S.Wilson
Key ref: M.Gamble et al. (2011). Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism. Proc Natl Acad Sci U S A, 108, 3536-3541. PubMed id: 21307308
Date:
20-Sep-10     Release date:   16-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
D0AB41  (D0AB41_ALKCL) -  Intracellular subtilisin protease from Alkalihalobacillus clausii
Seq:
Struc:
321 a.a.
301 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.62  - subtilisin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

 

 
Proc Natl Acad Sci U S A 108:3536-3541 (2011)
PubMed id: 21307308  
 
 
Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism.
M.Gamble, G.Künze, E.J.Dodson, K.S.Wilson, D.D.Jones.
 
  ABSTRACT  
 
No abstract given.

 

 

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