› 1qts

X-ray diffraction
1.4Å resolution

CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE

Released:
DOI: 10.2210/pdb1qts/pdb
PDB entry 1qts coloured by chain, front view.
PDB entry 1qts coloured by chain, side view.
PDB entry 1qts coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.
Traub LM, Downs MA, Westrich JL, Fremont DH
Proc Natl Acad Sci U S A 96 8907-12 (1999)
PMID: 10430869

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148055 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AP-2 complex subunit alpha-2 Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 27.83 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P17427 (Residues: 692-938; Coverage: 26%)
Gene names: Adtab, Ap2a2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 40.807Å b: 72.749Å c: 41.861Å
α: 90° β: 99.69° γ: 90°
R-values:
R R work R free
0.178 0.178 0.209
Expression system: Escherichia coli

Quick links

Citations

29 review citations

Biological basket weaving: formation and function of clathrin-coated vesicles.
Brodsky et al. (2001)
28 more

8 mentions without citation

Endocytic adaptors--social networking at the plasma membrane.
Reider et al. (2011)
7 more