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PDBsum entry 2vlc
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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2vlc

 

 

 

 

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Contents
Protein chains
518 a.a. *
Ligands
NAG-NAG ×6
BMA ×2
XYP ×2
Waters ×120
* Residue conservation analysis
PDB id:
2vlc
Name: Hydrolase
Title: Crystal structure of natural cinnamomin (isoform iii)
Structure: Ribosome-inactivating protein. Chain: a, b. Fragment: residues 11-580. Other_details: diacetyl-glucosamine (as5), mannose (bma) and xylose (xys)
Source: Cinnamomum camphora. Camphor tree. Organism_taxid: 13429. Organ: seeds. Other_details: natural
Resolution:
2.95Å     R-factor:   0.242     R-free:   0.309
Authors: A.Azzi,T.Wang,D.-W.Zhu,Y.-S.Zou,W.-Y.Liu,S.-X.Lin
Key ref:
A.Azzi et al. (2009). Crystal structure of native cinnamomin isoform III and its comparison with other ribosome inactivating proteins. Proteins, 74, 250-255. PubMed id: 18837036 DOI: 10.1002/prot.22251
Date:
11-Jan-08     Release date:   10-Feb-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q94BW3  (Q94BW3_CINCA) -  Ribosome-inactivating protein from Cinnamomum camphora
Seq:
Struc: 		 
Seq:
Struc: 		580 a.a.
518 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.2.22  - rRNA N-glycosylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

 

 
DOI no: 10.1002/prot.22251 Proteins 74:250-255 (2009)
PubMed id: 18837036  
 
 
Crystal structure of native cinnamomin isoform III and its comparison with other ribosome inactivating proteins.
A.Azzi, T.Wang, D.W.Zhu, Y.S.Zou, W.Y.Liu, S.X.Lin.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 2.
Figure 2. Polar and hydrophobic interactions across cinnamomin A and B-chains. Disulfide bridge between the two subunit is not visible in this view. 		Figure 3.
Figure 3. Active site residues of cinnamomin with 2FoFC electron density map contoured at 1.4 Binding residues tyrosine 75 and 115 surround wat118 which occupies a position where an adenine molecule is expected to be in the complex.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 74, 250-255) copyright 2009.  
  Figures were selected by an automated process.  

 

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