2JVA

NMR solution structure of peptidyl-tRNA hydrolase domain protein from Pseudomonas syringae pv. tomato. Northeast Structural Genomics Consortium target PsR211


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors.

Singarapu, K.K.Xiao, R.Acton, T.Rost, B.Montelione, G.T.Szyperski, T.

(2008) Proteins 71: 1027-1031

  • DOI: https://doi.org/10.1002/prot.21947
  • Primary Citation of Related Structures:  
    2JVA

  • PubMed Abstract: 

    The NMR structure of the peptidyl-tRNA hydrolase (PTH) domain from Pseudomonas syringae ( P. syringae PTH domain) was solved by using recently devised protocol for high throughput protein structure determination. The P. syringae PTH domain belongs to a large Pfam family PF00472, which consists of at least 1549 proteins annotated as ‘hydrolysis domains of peptidyl-tRNA’. The structure of P. syringae PTH domain expands the ‘structural coverage’ of the PFam family.


  • Organizational Affiliation

    Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260-3000, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Peptidyl-tRNA hydrolase domain protein108Pseudomonas syringae pv. tomato str. DC3000Mutation(s): 0 
Gene Names: PSPTO_1818
UniProt
Find proteins for Q885L4 (Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000))
Explore Q885L4 
Go to UniProtKB:  Q885L4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ885L4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-02
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2012-10-24
    Changes: Database references
  • Version 1.3: 2020-02-19
    Changes: Data collection, Database references, Other
  • Version 1.4: 2023-06-14
    Changes: Database references, Other