› 5u9j

X-ray diffraction
2.1Å resolution

Crystal structure of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) complexed with geranyl geranyl pyrophoshate

Released:
DOI: 10.2210/pdb5u9j/pdb
PDB entry 5u9j coloured by chain, front view.
PDB entry 5u9j coloured by chain, side view.
PDB entry 5u9j 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aryl-hydrocarbon-interacting protein-like 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 169 amino acids
Theoretical weight: 19.33 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

3 bound ligands:
Ligand GER 2 x GER
Ligand IPA 1 x IPA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 69.34Å b: 51.17Å c: 106.97Å
α: 90° β: 93.09° γ: 90°
R-values:
R R work R free
0.24 0.238 0.294
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Mutations in Hsp90 Cochaperones Result in a Wide Variety of Human Disorders.
Johnson JL. (2021)
1 more

4 mentions without citation

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