› 2xtn

X-ray diffraction
1.9Å resolution

Crystal structure of GTP-bound human GIMAP2, amino acid residues 1- 234

Released:
DOI: 10.2210/pdb2xtn/pdb
PDB entry 2xtn coloured by chain, front view.
PDB entry 2xtn coloured by chain, side view.
PDB entry 2xtn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).
Schwefel D, Fröhlich C, Eichhorst J, Wiesner B, Behlke J, Aravind L, Daumke O
Proc Natl Acad Sci U S A 107 20299-304 (2010)
PMID: 21059949

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase IMAP family member 2 Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 25.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UG22 (Residues: 1-234; Coverage: 69%)
Gene names: GIMAP2, IMAP2
Sequence domains: AIG1 family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand GTP 1 x GTP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 58.01Å b: 69.2Å c: 116.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.221
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

3 mentions without citation

Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).
Schwefel et al. (2010)
2 more