› 4iqc

X-ray diffraction
1.9Å resolution

P3121 crystal form of FKBP12.6

Released:
DOI: 10.2210/pdb4iqc/pdb
PDB entry 4iqc coloured by chain, front view.
PDB entry 4iqc coloured by chain, side view.
PDB entry 4iqc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6.
Chen H, Mustafi SM, LeMaster DM, Li Z, Héroux A, Li H, Hernández G
Acta Crystallogr D Biol Crystallogr 70 636-46 (2014)
PMID: 24598733

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1B Chains: A, B
Molecule details ›
Chains: A, B
Length: 107 amino acids
Theoretical weight: 11.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68106 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP12.6, FKBP1B, FKBP1L, FKBP9, OTK4
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3121
Unit cell:
a: 52.816Å b: 52.816Å c: 152.949Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.195 0.222
Expression system: Escherichia coli

Quick links

Citations

3 mentions without citation

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