Structure analysis

Functional architecture of the retromer cargo-recognition complex

X-ray diffraction
2.8Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dimer
Accessible surface area: 21100 Å2
Buried surface area: 3200 Å2
Dissociation area: 1,600 Å2
Dissociation energy (ΔGdiss): 8 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -16 kcal/mol
Symmetry number: 1
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 21000 Å2
Buried surface area: 3600 Å2
Dissociation area: 1,600 Å2
Dissociation energy (ΔGdiss): 4 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -13 kcal/mol
Symmetry number: 1

Macromolecules

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
Pfam: Calcineurin-like phosphoesterase superfamily domain
InterPro:
CATH: Purple Acid Phosphatase; chain A, domain 2
SCOP: YfcE-like

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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
InterPro:

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