› 2mph

Solution NMR

Solution Structure of human FK506 binding Protein 25

Released:
DOI: 10.2210/pdb2mph/pdb
PDB entry 2mph coloured by chain, ensemble of 20 models, front view.
PDB entry 2mph coloured by chain, ensemble of 20 models, side view.
PDB entry 2mph coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin.
Prakash A, Shin J, Rajan S, Yoon HS
OpenAccess logo Nucleic Acids Res 44 2909-25 (2016)
PMID: 26762975

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP3 Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 25.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00688 (Residues: 1-224; Coverage: 100%)
Gene names: FKBP25, FKBP3
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

FKBP Ligands-Where We Are and Where to Go?
Kolos et al. (2018)
4 more

7 mentions without citation

Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations.
Brodie et al. (2017)
6 more