› 2b92

X-ray diffraction
3.2Å resolution

Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GDP/AlF3

Released:
DOI: 10.2210/pdb2b92/pdb
PDB entry 2b92 coloured by chain, front view.
PDB entry 2b92 coloured by chain, side view.
PDB entry 2b92 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP.
Ghosh A, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C
Nature 440 101-4 (2006)
PMID: 16511497

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152321 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 37.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P32455 (Residues: 1-317; Coverage: 54%)
Gene name: GBP1
Sequence domains: Guanylate-binding protein, N-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand GDP 2 x GDP
Ligand AF3 2 x AF3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 148.82Å b: 103.921Å c: 55.485Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.25
Expression system: Escherichia coli BL21

Quick links

Citations

27 review citations

Dynamin, a membrane-remodelling GTPase.
Ferguson et al. (2012)
26 more

17 mentions without citation

Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Daumke et al. (2016)
16 more