PDBsum entry 1v0n

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protein ligands links
Hydrolase PDB id
Protein chain
302 a.a. *
EDO ×2
Waters ×618
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Xylanase xyn10a from streptomyces lividans in complex with xylobio-isofagomine at ph 7.5
Structure: Endo-1,4-beta-xylanase a. Chain: a. Fragment: catalytic module, residues 42-354. Synonym: xylanase a, 1,4-beta-d-xylan xylanohydrolase a. Engineered: yes
Source: Streptomyces lividans. Organism_taxid: 1916. Expressed in: streptomyces lividans. Expression_system_taxid: 1916.
1.10Å     R-factor:   0.104     R-free:   0.124
Authors: T.M.Gloster,S.J.Williams,S.Roberts,C.A.Tarling,J.Wicki, S.G.Withers,G.J.Davies
Key ref: T.M.Gloster et al. (2004). Atomic resolution analyses of the binding of xylobiose-derived deoxynojirimycin and isofagomine to xylanase Xyn10A. Chem Commun (Camb), 16, 1794-1795. PubMed id: 15306887
31-Mar-04     Release date:   16-Aug-04    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P26514  (XYNA_STRLI) -  Endo-1,4-beta-xylanase A
477 a.a.
302 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Endo-1,4-beta-xylanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  


Chem Commun (Camb) 16:1794-1795 (2004)
PubMed id: 15306887  
Atomic resolution analyses of the binding of xylobiose-derived deoxynojirimycin and isofagomine to xylanase Xyn10A.
T.M.Gloster, S.J.Williams, S.Roberts, C.A.Tarling, J.Wicki, S.G.Withers, G.J.Davies.
The atomic resolution structures of xylobiose-derived isofagomine and xylobiose-derived deoxynojirimycin in complex with the xylanase Xyn10A from Streptomyces lividans reveal undistorted (4)C(1) chair conformed sugars and, in the case of the deoxynojirimycin analogue, suggest unusual pK(a) changes of the enzyme's catalytic machinery upon binding.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19532990 M.Aguilar-Moncayo, T.M.Gloster, J.P.Turkenburg, M.I.García-Moreno, C.Ortiz Mellet, G.J.Davies, and J.M.García Fernández (2009).
Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.
  Org Biomol Chem, 7, 2738-2747.
PDB codes: 2wbg 2wc3 2wc4
18074341 A.D.Hill, and P.J.Reilly (2008).
A Gibbs free energy correlation for automated docking of carbohydrates.
  J Comput Chem, 29, 1131-1141.  
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