PDBe 4hlq

X-ray diffraction
3.3Å resolution

Crystal structure of human rab1b bound to GDP and BEF3 in complex with the GAP domain of TBC1D20 from homo sapiens

Released:
Source organism: Homo sapiens
Primary publication:
Catalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detail.
Proc. Natl. Acad. Sci. U.S.A. 109 21348-53 (2012)
PMID: 23236136

Function and Biology Details

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):
TBC1 domain family member 20 Chains: A, C, E, G, I
Molecule details ›
Chains: A, C, E, G, I
Length: 305 amino acids
Theoretical weight: 34.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96BZ9 (Residues: 1-305; Coverage: 76%)
Gene names: C20orf140, TBC1D20
Sequence domains: Rab-GTPase-TBC domain
Structure domains:
Ras-related protein Rab-1B Chains: B, D, F, H, J
Molecule details ›
Chains: B, D, F, H, J
Length: 175 amino acids
Theoretical weight: 19.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H0U4 (Residues: 3-174; Coverage: 86%)
Gene name: RAB1B
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 88.17Å b: 118.64Å c: 290.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.274
Expression system: Escherichia coli