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PDBsum entry 2jg0

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protein ligands links
Hydrolase PDB id
2jg0
Jmol
Contents
Protein chain
507 a.a. *
Ligands
TTZ
Waters ×676
* Residue conservation analysis
PDB id:
2jg0
Name: Hydrolase
Title: Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin
Structure: Periplasmic trehalase. Chain: a. Fragment: residues 31-565. Synonym: alpha alpha-trehalase, alpha alpha-trehalose glucohydrolase, trehalase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.50Å     R-factor:   0.149     R-free:   0.189
Authors: R.P.Gibson,T.M.Gloster,S.Roberts,R.A.J.Warren, I.Storch De Gracia,A.Garcia,J.L.Chiara,G.J.Davies
Key ref: R.P.Gibson et al. (2007). Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors. Angew Chem Int Ed Engl, 46, 4115-4119. PubMed id: 17455176
Date:
07-Feb-07     Release date:   13-Feb-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13482  (TREA_ECOLI) -  Periplasmic trehalase
Seq:
Struc:
 
Seq:
Struc:
565 a.a.
507 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.28  - Alpha,alpha-trehalase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
Alpha,alpha-trehalose
+ H(2)O
=
beta-D-glucose
Bound ligand (Het Group name = TTZ)
matches with 42.00% similarity
+ alpha-D-glucose
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     periplasmic space   2 terms 
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
Angew Chem Int Ed Engl 46:4115-4119 (2007)
PubMed id: 17455176  
 
 
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors.
R.P.Gibson, T.M.Gloster, S.Roberts, R.A.Warren, I.Storch de Gracia, A.García, J.L.Chiara, G.J.Davies.
 
  ABSTRACT  
 
No abstract given.