› 2r17

X-ray diffraction
2.8Å resolution

Functional architecture of the retromer cargo-recognition complex

Released:
DOI: 10.2210/pdb2r17/pdb
PDB entry 2r17 coloured by chain, front view.
PDB entry 2r17 coloured by chain, side view.
PDB entry 2r17 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional architecture of the retromer cargo-recognition complex.
Hierro A, Rojas AL, Rojas R, Murthy N, Effantin G, Kajava AV, Steven AC, Bonifacino JS, Hurley JH
Nature 449 1063-7 (2007)
PMID: 17891154

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188702 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vacuolar protein sorting-associated protein 29 Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UBQ0 (Residues: 1-182; Coverage: 100%)
Gene names: DC15, DC7, MDS007, VPS29
Sequence domains: Calcineurin-like phosphoesterase superfamily domain
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Vacuolar protein sorting-associated protein 35 Chains: C, D
Molecule details ›
Chains: C, D
Length: 298 amino acids
Theoretical weight: 34.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96QK1 (Residues: 483-780; Coverage: 37%)
Gene names: MEM3, TCCCTA00141, VPS35
Sequence domains: Vacuolar protein sorting-associated protein 35
Structure domains: Vacuolar protein sorting-associated protein 35, helical subcomplex Vps35-C

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 66.25Å b: 128.471Å c: 140.452Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

58 review citations

Tracing the retrograde route in protein trafficking.
Johannes et al. (2008)
57 more

18 mentions without citation

Retromer.
Bonifacino et al. (2008)
17 more