› 1q1c

X-ray diffraction
1.9Å resolution

Crystal structure of N(1-260) of human FKBP52

Released:
DOI: 10.2210/pdb1q1c/pdb
PDB entry 1q1c coloured by chain, front view.
PDB entry 1q1c coloured by chain, side view.
PDB entry 1q1c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.
Wu B, Li P, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, Rao Z
Proc Natl Acad Sci U S A 101 8348-53 (2004)
PMID: 15159550

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02790 (Residues: 2-260; Coverage: 56%)
Gene names: FKBP4, FKBP52
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

2 bound ligands:
Ligand DMS 5 x DMS
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P21
Unit cell:
a: 48.829Å b: 42.218Å c: 79.065Å
α: 90° β: 102.25° γ: 90°
R-values:
R R work R free
0.211 0.208 0.247
Expression system: Escherichia coli

Quick links

Citations

22 review citations

How corticosteroids control inflammation: Quintiles Prize Lecture 2005.
Barnes PJ. (2006)
21 more

21 mentions without citation

FKBP51 and FKBP52 in signaling and disease.
Storer et al. (2011)
20 more