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PDBsum entry 3zr5

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protein ligands metals links
Hydrolase PDB id
3zr5
Jmol
Contents
Protein chain
641 a.a.
Ligands
NAG ×7
Metals
_CA
Waters ×258
PDB id:
3zr5
Name: Hydrolase
Title: Structure of galactocerebrosidase from mouse
Structure: Galactocerebrosidase. Chain: a. Fragment: residues 40-684. Synonym: galcerase, galactocerebroside beta-galactosidase, galactosylceramidase, galactosylceramide beta-galactosidas engineered: yes. Other_details: fragment corresponds to residues 25-668 base numbering starting at second uniprot initiation site
Source: Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293 cells.
Resolution:
2.10Å     R-factor:   0.182     R-free:   0.214
Authors: J.E.Deane,S.C.Graham,N.N.Kim,P.E.Stein,R.Mcnair,M.B.Cachon-G T.M.Cox,R.J.Read
Key ref: J.E.Deane et al. (2011). Insights into Krabbe disease from structures of galactocerebrosidase. Proc Natl Acad Sci U S A, 108, 15169-15173. PubMed id: 21876145
Date:
14-Jun-11     Release date:   28-Sep-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P54818  (GALC_MOUSE) -  Galactocerebrosidase
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: D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine
D-galactosyl-N-acylsphingosine
+ H(2)O
=
D-galactose
Bound ligand (Het Group name = NAG)
matches with 62.50% similarity
+ N-acylsphingosine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   2 terms 
  Biochemical function     galactosylceramidase activity     1 term  

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 108:15169-15173 (2011)
PubMed id: 21876145  
 
 
Insights into Krabbe disease from structures of galactocerebrosidase.
J.E.Deane, S.C.Graham, N.N.Kim, P.E.Stein, R.McNair, M.B.Cachón-González, T.M.Cox, R.J.Read.
 
  ABSTRACT  
 
No abstract given.