› 2oev

X-ray diffraction
3.3Å resolution

Crystal structure of ALIX/AIP1

Released:
DOI: 10.2210/pdb2oev/pdb
PDB entry 2oev coloured by chain, front view.
PDB entry 2oev coloured by chain, side view.
PDB entry 2oev coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.
Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP
Cell 128 841-52 (2007)
PMID: 17350572

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186719 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Programmed cell death 6-interacting protein Chain: A
Molecule details ›
Chain: A
Length: 705 amino acids
Theoretical weight: 78.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WUM4 (Residues: 1-698; Coverage: 80%)
Gene names: AIP1, ALIX, KIAA1375, PDCD6IP
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 143.993Å b: 98.51Å c: 72.159Å
α: 90° β: 105.64° γ: 90°
R-values:
R R work R free
0.24 0.235 0.317
Expression system: Escherichia coli

Quick links

Citations

62 review citations

Specificities of secretion and uptake of exosomes and other extracellular vesicles for cell-to-cell communication.
Mathieu et al. (2019)
61 more

8 mentions without citation

HIV-1 assembly, budding, and maturation.
Sundquist et al. (2012)
7 more