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protein metals Protein-protein interface(s) links
Glycosyl hydrolase PDB id
1ups
Jmol
Contents
Protein chains
402 a.a. *
Metals
_CA ×2
Waters ×378
* Residue conservation analysis
PDB id:
1ups
Name: Glycosyl hydrolase
Title: Glcnac[alpha]1-4gal releasing endo-[beta]-galactosidase from clostridium perfringens
Structure: Glcnac-alpha-1,4-gal-releasing endo-beta- galactosidase. Chain: a, b. Engineered: yes
Source: Clostridium perfringens. Organism_taxid: 1502. Atcc: 10543. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.82Å     R-factor:   0.177     R-free:   0.204
Authors: W.Tempel,Z.-J.Liu,P.S.Horanyi,L.Deng,D.Lee,M.G.Newton, J.P.Rose,H.Ashida,S.-C.Li,Y.-T.Li,B.-C.Wang, Southeast Collaboratory For Structural Genomics (Secsg)
Key ref:
W.Tempel et al. (2005). Three-dimensional structure of GlcNAcalpha1-4Gal releasing endo-beta-galactosidase from Clostridium perfringens. Proteins, 59, 141-144. PubMed id: 15688452 DOI: 10.1002/prot.20363
Date:
10-Oct-03     Release date:   25-Nov-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q934G8  (Q934G8_CLOPE) -  GlcNAc-alpha-1,4-Gal-releasing endo-beta-galactosidase
Seq:
Struc:
420 a.a.
402 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  

 

 
DOI no: 10.1002/prot.20363 Proteins 59:141-144 (2005)
PubMed id: 15688452  
 
 
Three-dimensional structure of GlcNAcalpha1-4Gal releasing endo-beta-galactosidase from Clostridium perfringens.
W.Tempel, Z.J.Liu, P.S.Horanyi, L.Deng, D.Lee, M.G.Newton, J.P.Rose, H.Ashida, S.C.Li, Y.T.Li, B.C.Wang.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Stereographic cartoon of the Endo- -Gal[GnGa] molecule. The partially disordered loop connecting the 2 globular domains is represented as a dashed line.
Figure 2.
Figure 2. The -strand topology of Endo- -Gal[GNGa]. The larger N-terminal domain consists of a -sheet sandwich. The smaller C-terminal domain is an assembly of 6 double-stranded sheets. For clarity, the length of strand symbols and linkers do not represent their relative sizes in the peptide. Coloring roughly corresponds to that in Figure 1.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 59, 141-144) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18703845 T.Y.Hong, Y.Y.Hsiao, M.Meng, and T.T.Li (2008).
The 1.5 A structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1,3-beta-glucan-binding specificity and hydrolysis.
  Acta Crystallogr D Biol Crystallogr, 64, 964-970.
PDB code: 3dgt
16550377 G.Michel, P.Nyval-Collen, T.Barbeyron, M.Czjzek, and W.Helbert (2006).
Bioconversion of red seaweed galactans: a focus on bacterial agarases and carrageenases.
  Appl Microbiol Biotechnol, 71, 23-33.  
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 code is shown on the right.