› 5u9a

X-ray diffraction
2.7Å resolution

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

Released:
DOI: 10.2210/pdb5u9a/pdb
PDB entry 5u9a coloured by chain, front view.
PDB entry 5u9a coloured by chain, side view.
PDB entry 5u9a 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 Chain: A
Molecule details ›
Chain: A
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2221
Unit cell:
a: 52.1Å b: 65.74Å c: 107.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.212 0.289
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mutations in Hsp90 Cochaperones Result in a Wide Variety of Human Disorders.
Johnson JL. (2021)
7 other articles

5 mentions without citation

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