› 6vaq

X-ray diffraction
2.95Å resolution

Crystal structure of glucose-6-phosphate dehydrogenase V394L mutant in complex with catalytic NADP+

Released:
DOI: 10.2210/pdb6vaq/pdb
PDB entry 6vaq coloured by chain, front view.
PDB entry 6vaq coloured by chain, side view.
PDB entry 6vaq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Long-range structural defects by pathogenic mutations in most severe glucose-6-phosphate dehydrogenase deficiency.
Horikoshi N, Hwang S, Gati C, Matsui T, Castillo-Orellana C, Raub AG, Garcia AA, Jabbarpour F, Batyuk A, Broweleit J, Xiang X, Chiang A, Broweleit R, Vöhringer-Martinez E, Mochly-Rosen D, Wakatsuki S
Proc Natl Acad Sci U S A 118 (2021)
PMID: 33468660

Function and Biology Details

Reaction catalysed: 
D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate 1-dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 515 amino acids
Theoretical weight: 59.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11413 (Residues: 1-515; Coverage: 100%)
Gene name: G6PD
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P41212
Unit cell:
a: 158.973Å b: 158.973Å c: 113.186Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.209 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Treatment strategies for glucose-6-phosphate dehydrogenase deficiency: past and future perspectives.
Garcia et al. (2021)
3 more

1 mention without citation

Stabilization of glucose-6-phosphate dehydrogenase oligomers enhances catalytic activity and stability of clinical variants.
Garcia et al. (2022)