PDBsum entry 2ofn

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protein links
Isomerase PDB id
Protein chain
135 a.a. *
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Solution structure of fk506-binding domain (fkbd)of fkbp35 f plasmodium falciparum
Structure: 70 kda peptidylprolyl isomerase, putative. Chain: a. Fragment: fk-506 binding domain. Synonym: fkbp35, fk506-binding protein 35. Engineered: yes
Source: Plasmodium falciparum. Organism_taxid: 36329. Strain: 3d7. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: C.B.Kang,H.Ye,H.R.Yoon,H.S.Yoon
Key ref:
C.B.Kang et al. (2008). Solution structure of FK506 binding domain (FKBD) of Plasmodium falciparum FK506 binding protein 35 (PfFKBP35). Proteins, 70, 300-302. PubMed id: 17876830 DOI: 10.1002/prot.21623
04-Jan-07     Release date:   25-Dec-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q8I4V8  (Q8I4V8_PLAF7) -  FK506-binding protein (FKBP)-type peptidyl-propyl isomerase
304 a.a.
135 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   1 term 


    Added reference    
DOI no: 10.1002/prot.21623 Proteins 70:300-302 (2008)
PubMed id: 17876830  
Solution structure of FK506 binding domain (FKBD) of Plasmodium falciparum FK506 binding protein 35 (PfFKBP35).
C.B.Kang, H.Ye, H.R.Yoon, H.S.Yoon.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. NMR structure of FKBD of PfFKBP35. A: Sequence alignment of FKBD of PfFKBP35 (AAN36539) and FKBP12 (A35780). Protein sequence alignment was generated by Vector NTI Align X (Informax). Based on three-dimensional structure of FKBP/FK506,[5] residues in the active pocket for binding FK506 are indicated by open reverse triangles, and those which are involved in interaction with FK506 through hydrogen bonding are indicated by filled circles. NCBI protein data base accession number is indicated in parenthesis. The identical residues and residues with conservative changes are shown in orange and green, respectively. B: Backbone ensemble of 20 conformers with lowest energy is shown superposed. Ribbon drawings of FKBD of PfFKBP35 (C) and FKBP12 (PDB: 1FKS) (D) are displayed, respectively. E: An overlay of the backbone heavy atom trace (N, C ,C ^) of the NMR structures of FKBP12 (Red) and FKBD of PfFKBP35 (Blue) is shown.
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 70, 300-302) copyright 2008.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20572013 R.Alag, I.A.Qureshi, N.Bharatham, J.Shin, J.Lescar, and H.S.Yoon (2010).
NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35.
  Protein Sci, 19, 1577-1586.
PDB code: 3ihz
19691130 R.Alag, N.Bharatham, A.Dong, T.Hills, A.Harikishore, A.A.Widjaja, S.G.Shochat, R.Hui, and H.S.Yoon (2009).
Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
  Protein Sci, 18, 2115-2124.
PDB code: 2fbn
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