› 2bme

X-ray diffraction
1.57Å resolution

high resolution structure of GppNHp-bound human Rab4a

Released:
DOI: 10.2210/pdb2bme/pdb
PDB entry 2bme coloured by chain, front view.
PDB entry 2bme coloured by chain, side view.
PDB entry 2bme coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High resolution crystal structures of human Rab4a in its active and inactive conformations.
Huber SK, Scheidig AJ
FEBS Lett 579 2821-9 (2005)
PMID: 15907487

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras-related protein Rab-4A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 186 amino acids
Theoretical weight: 20.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20338 (Residues: 6-189; Coverage: 84%)
Gene names: RAB4, RAB4A
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand GNP 4 x GNP
Ligand TRS 4 x TRS
Ligand BME 2 x BME
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43
Unit cell:
a: 99.79Å b: 99.79Å c: 95.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Molecular control of Rab activity by GEFs, GAPs and GDI.
Müller et al. (2018)
2 more

7 mentions without citation

Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.
Pylypenko et al. (2018)
6 more