› 2duu

X-ray diffraction
2.9Å resolution

Crystal Structure of apo-form of NADP-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase from Synechococcus Sp.

Released:
DOI: 10.2210/pdb2duu/pdb
PDB entry 2duu coloured by chain, front view.
PDB entry 2duu coloured by chain, side view.
PDB entry 2duu coloured by chain, top view.
Source organism: Synechococcus elongatus PCC 7942 = FACHB-805
Primary publication:
Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.
Kitatani T, Nakamura Y, Wada K, Kinoshita T, Tamoi M, Shigeoka S, Tada T
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 727-30 (2006)
PMID: 16880542

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193113 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: A, B, O, P, Q, R
Molecule details ›
Chains: A, B, O, P, Q, R
Length: 380 amino acids
Theoretical weight: 41.38 KDa
Source organism: Synechococcus elongatus PCC 7942 = FACHB-805
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9R6W2 (Residues: 1-336; Coverage: 99%)
Gene names: Synpcc7942_1742, gap2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: C2
Unit cell:
a: 151.4Å b: 79.8Å c: 207.2Å
α: 90° β: 102.1° γ: 90°
R-values:
R R work R free
0.217 0.217 0.275
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.
Kim YJ. (2018)
1 more

1 mention without citation

Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.
Kitatani et al. (2006)