1tu3

X-ray diffraction
2.31Å resolution

Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Rab-5A Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 171 amino acids
Theoretical weight: 19.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20339 (Residues: 14-184; Coverage: 80%)
Gene names: RAB5, RAB5A
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Rab GTPase-binding effector protein 1 Chains: F, G, H, I, J
Molecule details ›
Chains: F, G, H, I, J
Length: 79 amino acids
Theoretical weight: 9.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15276 (Residues: 789-862; Coverage: 9%)
Gene names: RAB5EP, RABEP1, RABPT5, RABPT5A
Structure domains: Single helix bin

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 112.4Å b: 83.5Å c: 144.9Å
α: 90° β: 102.2° γ: 90°
R-values:
R R work R free
0.222 0.222 0.277
Expression system: Escherichia coli BL21(DE3)