› 3jxv

X-ray diffraction
2.08Å resolution

Crystal Structure of the 3 FKBP domains of wheat FKBP73

Released:
DOI: 10.2210/pdb3jxv/pdb
PDB entry 3jxv coloured by chain, front view.
PDB entry 3jxv coloured by chain, side view.
PDB entry 3jxv coloured by chain, top view.
Source organism: Triticum aestivum
Primary publication:
Crystal structure of the three FK506 binding protein domains of wheat FKBP73: evidence for a unique wFK73_2 domain.
Unger T, Dym O, Albeck S, Jacobovitch Y, Bernehim R, Marom D, Pisanty O, Breiman A
J Struct Funct Genomics 11 113-23 (2010)
PMID: 20306145

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174987 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
70 kDa peptidyl-prolyl isomerase Chain: A
Molecule details ›
Chain: A
Length: 356 amino acids
Theoretical weight: 39.13 KDa
Source organism: Triticum aestivum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43207 (Residues: 31-386; Coverage: 64%)
Gene name: FKBP70
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 69.168Å b: 31.322Å c: 96.716Å
α: 90° β: 98.46° γ: 90°
R-values:
R R work R free
0.251 0.248 0.287
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Functional diversity and pharmacological profiles of the FKBPs and their complexes with small natural ligands.
Galat A. (2013)
1 more

1 mention without citation

Automatic rebuilding and optimization of crystallographic structures in the Protein Data Bank.
Joosten et al. (2011)