› 4lav

X-ray diffraction
1.8Å resolution

Crystal Structure Analysis of FKBP52, Crystal Form II

Released:
DOI: 10.2210/pdb4lav/pdb
PDB entry 4lav coloured by chain, front view.
PDB entry 4lav coloured by chain, side view.
PDB entry 4lav coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the free and ligand-bound FK1-FK2 domain segment of FKBP52 reveal a flexible inter-domain hinge.
Bracher A, Kozany C, Hähle A, Wild P, Zacharias M, Hausch F
J Mol Biol 425 4134-44 (2013)
PMID: 23933011

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-169761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 27.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02790 (Residues: 16-260; Coverage: 53%)
Gene names: FKBP4, FKBP52
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 45.297Å b: 125.801Å c: 50.539Å
α: 90° β: 92.01° γ: 90°
R-values:
R R work R free
0.192 0.19 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

10 mentions without citation

Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.
Thapar R. (2015)
9 more