› 7b2g

X-ray diffraction
3Å resolution

Crystal structure of R120Q GDAP1 mutant

Released:
DOI: 10.2210/pdb7b2g/pdb
PDB entry 7b2g coloured by chain, front view.
PDB entry 7b2g coloured by chain, side view.
PDB entry 7b2g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conserved intramolecular networks in GDAP1 are closely connected to CMT-linked mutations and protein stability.
Sutinen A, Paffenholz D, Nguyen GTT, Ruskamo S, Torda AE, Kursula P
OpenAccess logo PLoS One 18 e0284532 (2023)
PMID: 37058526

Function and Biology Details

Biochemical function:
  • not assigned
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-186165 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ganglioside-induced differentiation-associated protein 1 Chain: A
Molecule details ›
Chain: A
Length: 302 amino acids
Theoretical weight: 35.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8TB36 (Residues: 1-302; Coverage: 84%)
Gene name: GDAP1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P6322
Unit cell:
a: 148.111Å b: 148.111Å c: 114.538Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.23 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Conserved intramolecular networks in GDAP1 are closely connected to CMT-linked mutations and protein stability.
Sutinen et al. (2023)