PDBe 3l0i

X-ray diffraction
2.85Å resolution

Complex structure of SidM/DrrA with the wild type Rab1

Primary publication:
Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA.
Proc. Natl. Acad. Sci. U.S.A. 107 4699-704 (2010)
PMID: 20176951

Function and Biology Details

Reactions catalysed:
ATP + [protein]-L-threonine = diphosphate + [protein]-O(4)-(5'-adenylyl)-L-threonine
GTP + [protein]-L-tyrosine = diphosphate + [protein]-O(4)-(5'-guanylyl)-L-tyrosine
Biochemical function:
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):
Multifunctional virulence effector protein DrrA Chains: A, C
Molecule details ›
Chains: A, C
Length: 363 amino acids
Theoretical weight: 41.82 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
  • Canonical: Q5ZSQ3 (Residues: 193-550; Coverage: 55%)
Gene names: drrA, lpg2464, sidM
Structure domains:
Ras-related protein Rab-1A Chains: B, D
Molecule details ›
Chains: B, D
Length: 199 amino acids
Theoretical weight: 22.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P62820 (Residues: 1-177; Coverage: 86%)
Gene names: RAB1, RAB1A
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 63.808Å b: 71.747Å c: 146.911Å
α: 90° β: 93.62° γ: 90°
R R work R free
0.262 0.226 0.266
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21(DE3)