2G0Q

Solution structure of At5g39720.1 from Arabidopsis thaliana


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family.

Lytle, B.L.Peterson, F.C.Tyler, E.M.Newman, C.L.Vinarov, D.A.Markley, J.L.Volkman, B.F.

(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 490-493

  • DOI: https://doi.org/10.1107/S1744309106015946
  • Primary Citation of Related Structures:  
    2G0Q

  • PubMed Abstract: 

    The three-dimensional structure of Arabidopsis thaliana protein At5g39720.1 was determined by NMR spectroscopy. It is the first representative structure of Pfam family PF06094, which contains protein sequences similar to that of AIG2, an A. thaliana protein of unknown function induced upon infection by the bacterial pathogen Pseudomonas syringae. The At5g39720.1 structure consists of a five-stranded beta-barrel surrounded by two alpha-helices and a small beta-sheet. A long flexible alpha-helix protrudes from the structure at the C-terminal end. A structural homology search revealed similarity to three members of Pfam family UPF0131. Conservation of residues in a hydrophilic cavity able to bind small ligands in UPF0131 proteins suggests that this may also serve as an active site in AIG2-like proteins.


  • Organizational Affiliation

    Center for Eukaryotic Structural Genomics, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
AT5G39720.1 protein173Arabidopsis thalianaMutation(s): 0 
Gene Names: At5g39720.1
UniProt
Find proteins for Q9FIX2 (Arabidopsis thaliana)
Explore Q9FIX2 
Go to UniProtKB:  Q9FIX2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9FIX2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-02-28
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-09
    Changes: Data collection, Database references, Derived calculations