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PDBsum entry 2zx9

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2zx9

 

 

 

 

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Contents
Protein chains
442 a.a. *
Ligands
ZX9 ×2
Waters ×391
* Residue conservation analysis
PDB id:
2zx9
Name: Hydrolase
Title: Alpha-l-fucosidase complexed with inhibitor, b4
Structure: Alpha-l-fucosidase, putative. Chain: a, b. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Strain: msb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.62Å     R-factor:   0.162     R-free:   0.227
Authors: H.-J.Wu,T.-P.Ko,C.-W.Ho,C.-H.Lin,A.H.-J.Wang
Key ref: H.J.Wu et al. (2010). Structural basis of alpha-fucosidase inhibition by iminocyclitols with K(i) values in the micro- to picomolar range. Angew Chem Int Ed Engl, 49, 337-340. PubMed id: 19967696
Date:
22-Dec-08     Release date:   08-Dec-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9WYE2  (Q9WYE2_THEMA) -  Alpha-L-fucosidase, putative from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Seq:
Struc:
449 a.a.
442 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.51  - alpha-L-fucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: an alpha-L-fucoside + H2O = L-fucose + an alcohol
alpha-L-fucoside
+ H2O
= L-fucose
+ alcohol
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Angew Chem Int Ed Engl 49:337-340 (2010)
PubMed id: 19967696  
 
 
Structural basis of alpha-fucosidase inhibition by iminocyclitols with K(i) values in the micro- to picomolar range.
H.J.Wu, C.W.Ho, T.P.Ko, S.D.Popat, C.H.Lin, A.H.Wang.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20665773 A.Lammerts van Bueren, S.D.Popat, C.H.Lin, and G.J.Davies (2010).
Structural and thermodynamic analyses of α-L-fucosidase inhibitors.
  Chembiochem, 11, 1971-1974.
PDB codes: 2xib 2xii
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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