› 5bxj

X-ray diffraction
1.24Å resolution

Complex of the Fk1 domain mutant A19T of FKBP51 with 4-Nitrophenol

Released:
DOI: 10.2210/pdb5bxj/pdb
PDB entry 5bxj coloured by chain, front view.
PDB entry 5bxj coloured by chain, side view.
PDB entry 5bxj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The environmental endocrine disruptor p-nitrophenol interacts with FKBP51, a positive regulator of androgen receptor and inhibits androgen receptor signaling in human cells.
Wu D, Tao X, Chen ZP, Han JT, Jia WJ, Zhu N, Li X, Wang Z, He YX
J Hazard Mater 307 193-201 (2016)
PMID: 26780698

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-171693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP5 Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13451 (Residues: 16-140; Coverage: 27%)
Gene names: AIG6, FKBP5, FKBP51
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 42.127Å b: 53.72Å c: 56.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.206
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52
Zgajnar et al. (2019)
1 more

1 mention without citation

Determining novel candidate anti-hepatocellular carcinoma drugs using interaction networks and molecular docking between drug targets and natural compounds of SiNiSan.
Zhang et al. (2021)