1tu4

X-ray diffraction
2.2Å resolution

Crystal Structure of Rab5-GDP Complex

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of Rab5-Rabaptin5 interaction in endocytosis.
Nat Struct Mol Biol 11 975-83 (2004)
PMID: 15378032

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
homo octamer
homo tetramer
PDBe Complex ID:
PDB-CPX-148944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras-related protein Rab-5A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 171 amino acids
Theoretical weight: 19.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20339 (Residues: 14-184; Coverage: 80%)
Gene names: RAB5, RAB5A
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CAMD BEAMLINE GCPCC
Spacegroup: P3121
Unit cell:
a: 84.9Å b: 84.9Å c: 199.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.217 0.274
Expression system: Escherichia coli