› 5v35

X-ray diffraction
2.5Å resolution

Crystal structure of V71F mutant of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) complexed with S-farnesyl-L-cysteine methyl ester

Released:
DOI: 10.2210/pdb5v35/pdb
PDB entry 5v35 coloured by chain, front view.
PDB entry 5v35 coloured by chain, side view.
PDB entry 5v35 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Unique structural features of the AIPL1-FKBP domain that support prenyl lipid binding and underlie protein malfunction in blindness.
Yadav RP, Gakhar L, Yu L, Artemyev NO
Proc Natl Acad Sci U S A 114 E6536-E6545 (2017)
PMID: 28739921

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aryl-hydrocarbon-interacting protein-like 1 Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NZN9 (Residues: 2-161; Coverage: 42%)
Gene names: AIPL1, AIPL2

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2221
Unit cell:
a: 53.15Å b: 65.52Å c: 106.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.216 0.272
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

1 mention without citation

Unique structural features of the AIPL1-FKBP domain that support prenyl lipid binding and underlie protein malfunction in blindness.
Yadav et al. (2017)