5o74

X-ray diffraction
2.5Å resolution

Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP

Released:

Function and Biology Details

Reactions catalysed:
GTP + [protein]-L-tyrosine = diphosphate + [protein]-O(4)-(5'-guanylyl)-L-tyrosine
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-173366 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Multifunctional virulence effector protein DrrA Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 197 amino acids
Theoretical weight: 22 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q29ST3 (Residues: 340-533; Coverage: 30%)
Gene names: drrA, sidM
Sequence domains: SidM, Rab1-activation domain
Structure domains: Ferritin
Ras-related protein Rab-1B Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 180 amino acids
Theoretical weight: 20.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H0U4 (Residues: 1-1, 3-174; Coverage: 86%)
Gene name: RAB1B
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P1
Unit cell:
a: 77.91Å b: 87.45Å c: 93.17Å
α: 114.61° β: 97.69° γ: 100.74°
R-values:
R R work R free
0.23 0.229 0.266
Expression system: Escherichia coli