› 2f2d

Solution NMR

Solution structure of the FK506-binding domain of human FKBP38

Released:
DOI: 10.2210/pdb2f2d/pdb
PDB entry 2f2d coloured by chain, ensemble of 20 models, front view.
PDB entry 2f2d coloured by chain, ensemble of 20 models, side view.
PDB entry 2f2d coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the FK506-binding domain of human FKBP38.
Maestre-Martínez M, Edlich F, Jarczowski F, Weiwad M, Fischer G, Lücke C
J Biomol NMR 34 197-202 (2006)
PMID: 16604427

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-171991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP8 Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14318 (Residues: 92-210; Coverage: 29%)
Gene names: FKBP38, FKBP8
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
Refinement method: simulated annealing combined with torsion angle dynamics followed by energy minimization
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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Bai et al. (2010)
1 more

3 mentions without citation

Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis.
Kliegman et al. (2006)
2 more