2KI3
Structural and biochemical characterization of FK506 binding domain from Plasmodium vivax
Summary for 2KI3
| Entry DOI | 10.2210/pdb2ki3/pdb |
| NMR Information | BMRB: 16260 |
| Descriptor | 70 kDa peptidylprolyl isomerase, putative (1 entity in total) |
| Functional Keywords | protein, isomerase, tpr repeat |
| Biological source | Plasmodium vivax |
| Total number of polymer chains | 1 |
| Total formula weight | 13971.69 |
| Authors | Alag, R.,Yoon, H.S.,Shin, J. (deposition date: 2009-04-21, release date: 2010-04-14, Last modification date: 2024-05-29) |
| Primary citation | Alag, R.,Shin, J.,Yoon, H.S. NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax Biomol.Nmr Assign., 3:243-245, 2009 Cited by 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. PubMed: 19774494DOI: 10.1007/s12104-009-9185-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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