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PDBsum entry 4ufh

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protein ligands metals links
Hydrolase PDB id
4ufh

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
641 a.a.
Ligands
NAG-NAG ×3
GIF
PG4
NAG
Metals
_NI ×2
_CA
Waters ×214
PDB id:
4ufh
Name: Hydrolase
Title: Mouse galactocerebrosidase complexed with iso-galacto-fagomine igf
Structure: Galactocerebrosidase. Chain: a. Synonym: galcerase, galactocerebroside beta-galactosidase, galactosylceramidase, galactosylceramide beta-galactosidase. Engineered: yes. Other_details: complex with igf
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293t
Resolution:
2.16Å     R-factor:   0.192     R-free:   0.216
Authors: C.H.Hill,A.H.Viuff,S.J.Spratley,S.Salamone,S.H.Christensen,R.J.Read, N.W.Moriarty,H.H.Jensen,J.E.Deane
Key ref: C.H.Hill et al. (2015). Azasugar inhibitors as pharmacological chaperones for Krabbe disease. Chem Sci, 6, 3075-3086. PubMed id: 26029356 DOI: 10.1039/c5sc00754b
Date:
17-Mar-15     Release date:   25-Mar-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P54818  (GALC_MOUSE) -  Galactocerebrosidase from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
684 a.a.
641 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.46  - galactosylceramidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-galactose
beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine
+ H2O
= N-acylsphing-4-enine
+
D-galactose
Bound ligand (Het Group name = NAG)
matches with 62.50% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1039/c5sc00754b Chem Sci 6:3075-3086 (2015)
PubMed id: 26029356  
 
 
Azasugar inhibitors as pharmacological chaperones for Krabbe disease.
C.H.Hill, A.H.Viuff, S.J.Spratley, S.Salamone, S.H.Christensen, R.J.Read, N.W.Moriarty, H.H.Jensen, J.E.Deane.
 
  ABSTRACT  
 
No abstract given.

 

 

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