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PDBsum entry 1vaj
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Structural genomics, unknown function PDB id
1vaj

 

 

 

 

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Contents
Protein chain
203 a.a. *
Waters ×165
* Residue conservation analysis
PDB id:
1vaj
Name: Structural genomics, unknown function
Title: Crystal structure of uncharacterized protein ph0010 from pyrococcus horikoshii
Structure: Hypothetical protein ph0010. Chain: a. Engineered: yes
Source: Pyrococcus horikoshii. Organism_taxid: 53953. Gene: ph0010. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.82Å     R-factor:   0.202     R-free:   0.232
Authors: Y.Tajika,N.Sakai,T.Tamura,M.Yao,N.Watanabe,I.Tanaka
Key ref:
Y.Tajika et al. (2005). Crystal structure of PH0010 from Pyrococcus horikoshii, which is highly homologous to human AMMECR 1C-terminal region. Proteins, 58, 501-503. PubMed id: 15558565 DOI: 10.1002/prot.20315
Date:
17-Feb-04     Release date:   25-Jan-05    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O57770  (Y010_PYRHO) -  Protein PH0010 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Seq:
Struc: 		206 a.a.
203 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1002/prot.20315 Proteins 58:501-503 (2005)
PubMed id: 15558565  
 
 
Crystal structure of PH0010 from Pyrococcus horikoshii, which is highly homologous to human AMMECR 1C-terminal region.
Y.Tajika, N.Sakai, T.Tamura, M.Yao, N.Watanabe, I.Tanaka.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. The 3D structure of PH0010. A: The ribbon representation of PH0010. B: The representation of the conserved residues. The side chains of conserved residues except for Gly are shown as a ball-and-stick model in red. The main chain of the large domain is shown in blue, and that of the small domain is shown in green. 		Figure 2.
Figure 2. Multiple sequence alignment of PH0010 and sequence homologues from four archaeas (Pyrococcus abyssi, Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Sulfolobus tokodaii), four bacteria (Aquifex aeolicus, Thermotoga maritime, Thermoanaerobacter tengcongensis, and Clostridium acetobutylicum), and five eukarya (Schizosaccharomyces pombe, Caenorhabditis elegans, Drosophila melanogaster, Mus musculus, and Homo sapiens). Completely conserved residues are colored in red, and highly conserved residues are colored in green.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 58, 501-503) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17715145 S.Balaji, and L.Aravind (2007).
The RAGNYA fold: a novel fold with multiple topological variants found in functionally diverse nucleic acid, nucleotide and peptide-binding proteins.
  Nucleic Acids Res, 35, 5658-5671.  
16111915 K.S.Makarova, and E.V.Koonin (2005).
Evolutionary and functional genomics of the Archaea.
  Curr Opin Microbiol, 8, 586-594.  
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.

 

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