4c4p

X-ray diffraction
2Å resolution

Crystal Structure of Wild-Type Rab11 Complexed to FIP2

Released:
Source organism: Homo sapiens
Entry authors: Sultana A, Khan AR

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Rab-11A Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 19.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62491 (Residues: 1-173; Coverage: 80%)
Gene names: RAB11, RAB11A
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Rab11 family-interacting protein 2 Chain: B
Molecule details ›
Chain: B
Length: 107 amino acids
Theoretical weight: 12.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7L804 (Residues: 410-512; Coverage: 20%)
Gene names: KIAA0941, RAB11FIP2
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3121
Unit cell:
a: 64.56Å b: 64.56Å c: 112.86Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.18 0.223
Expression system: Escherichia coli