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PDBsum entry 1rhx

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protein links
Transferase PDB id
1rhx
Jmol PyMol
Contents
Protein chain
87 a.a. *
* Residue conservation analysis
PDB id:
1rhx
Name: Transferase
Title: High-resolution nmr structure of a putative sulfur transfera (tm0979) from thermotoga maritima
Structure: Conserved hypothetical protein tm0979. Chain: a. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 20 models
Authors: W.Peti,T.Herrmann,K.Wuthrich,Joint Center For Structural Gen (Jcsg)
Key ref:
W.Peti et al. (2005). NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima. Proteins, 59, 387-390. PubMed id: 15723348 DOI: 10.1002/prot.20352
Date:
14-Nov-03     Release date:   21-Dec-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9X074  (Q9X074_THEMA) -  DsrH family protein
Seq:
Struc:
87 a.a.
87 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     tRNA wobble position uridine thiolation   1 term 

 

 
DOI no: 10.1002/prot.20352 Proteins 59:387-390 (2005)
PubMed id: 15723348  
 
 
NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.
W.Peti, T.Herrmann, O.Zagnitko, S.K.Grzechnik, K.Wüthrich.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. A: Stereo view of the bundle of 20 energy-minimized DYANA conformers representing the NMR structure of TM0979. The superposition is for best fit of the backbone atoms N, C^ and C of residues 3-85. The N- and C-terminal residues 1 and 87 are identified. B: Ribbon presentation of the closest conformer of TM0979 to the mean coordinates of the bundle of 20 conformers. The regular secondary structure elements are identified. C: Closest conformer of TM0979 to the mean coordinates of the bundle of 20 conformers. Color code: green, polypeptide backbone; blue, side chains with an average local displacement smaller than 0.85 Å; red, side chains with an average local displacement equal to or larger than 0.85 Å.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 59, 387-390) copyright 2005.  

 

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