2KI3

Structural and biochemical characterization of FK506 binding domain from Plasmodium vivax


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax

Alag, R.Shin, J.Yoon, H.S.

(2009) Biomol NMR Assign 3: 243-245

  • DOI: https://doi.org/10.1007/s12104-009-9185-1
  • Primary Citation of Related Structures:  
    2KI3

  • PubMed Abstract: 

    PvFKBP35 is a member of the FK506 binding protein family (FKBP) from Plasmodium vivax. The FK506-binding domain of PvFKBP35 shows a canonical peptidylprolyl cis-trans isomerase (PPIase) activity. To understand the role of PvFKBP35 in the parasite, we have performed NMR studies. Here, we report the assignment of the FK506-binding domain of PvFKBP35.


  • Organizational Affiliation

    School of Biological Science, Nanyang Technological University, Singapore, Singapore.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
70 kDa peptidylprolyl isomerase, putative126Plasmodium vivaxMutation(s): 0 
UniProt
Find proteins for A5K8X6 (Plasmodium vivax (strain Salvador I))
Explore A5K8X6 
Go to UniProtKB:  A5K8X6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA5K8X6
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 least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-04-14
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-16
    Changes: Data collection, Database references, Derived calculations