› 1f40

Solution NMR

SOLUTION STRUCTURE OF FKBP12 COMPLEXED WITH GPI-1046, A NEUROTROPHIC LIGAND

Released:
DOI: 10.2210/pdb1f40/pdb
PDB entry 1f40 coloured by chain, ensemble of 10 models, front view.
PDB entry 1f40 coloured by chain, ensemble of 10 models, side view.
PDB entry 1f40 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics.
Sich C, Improta S, Cowley DJ, Guenet C, Merly JP, Teufel M, Saudek V
Eur J Biochem 267 5342-55 (2000)
PMID: 10951192

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62942 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand GPI 1 x GPI
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design.
LeMaster et al. (2015)
1 more

11 mentions without citation

New Frontiers in Druggability.
Kozakov et al. (2015)
10 more