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PDBsum entry 3s5y

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protein ligands Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3s5y
Jmol
Contents
Protein chain
390 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-FUC-XYP
NAG-NAG-BMA-XYP-
FUC
NAG-NAG-FUC
DGJ ×2
2PE ×5
NAG
NAG-NAG-BMA-MAN-
XYP
NAG-NAG-BMA-FUC
EDO
ACY ×2
Waters ×440
PDB id:
3s5y
Name: Hydrolase/hydrolase inhibitor
Title: Pharmacological chaperoning in human alpha-galactosidase
Structure: Alpha-galactosidase a. Chain: a, b. Fragment: unp residues 32-429. Synonym: alpha-d-galactosidase a, alpha-d-galactoside galactohydrolase, melibiase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gla. Expressed in: nicotiana benthamiana. Expression_system_taxid: 4100
Resolution:
2.10Å     R-factor:   0.195     R-free:   0.230
Authors: A.I.Guce,N.E.Clark,S.C.Garman
Key ref: A.I.Guce et al. (2011). The molecular basis of pharmacological chaperoning in human α-galactosidase. Chem Biol, 18, 1521-1526. PubMed id: 22195554
Date:
23-May-11     Release date:   04-Jan-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P06280  (AGAL_HUMAN) -  Alpha-galactosidase A
Seq:
Struc:
429 a.a.
390 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.22  - Alpha-galactosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Melibiose + H2O = galactose + glucose

+
=
+
      Cofactor: Magnesium; NAD(+)
Magnesium
NAD(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   6 terms 
  Biological process     metabolic process   11 terms 
  Biochemical function     catalytic activity     10 terms  

 

 
    reference    
 
 
Chem Biol 18:1521-1526 (2011)
PubMed id: 22195554  
 
 
The molecular basis of pharmacological chaperoning in human α-galactosidase.
A.I.Guce, N.E.Clark, J.J.Rogich, S.C.Garman.
 
  ABSTRACT  
 
No abstract given.