› 2dbr

X-ray diffraction
2.61Å resolution

Crystal Structure of Glyoxylate Reductase (PH0597) from Pyrococcus horikoshii OT3, Complexed with NADP (P1)

Released:
DOI: 10.2210/pdb2dbr/pdb
PDB entry 2dbr coloured by chain, front view.
PDB entry 2dbr coloured by chain, side view.
PDB entry 2dbr coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate.
Yoshikawa S, Arai R, Kinoshita Y, Uchikubo-Kamo T, Wakamatsu T, Akasaka R, Masui R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S
Acta Crystallogr D Biol Crystallogr 63 357-65 (2007)
PMID: 17327673

Function and Biology Details

Reaction catalysed: 
Glycolate + NAD(+) = glyoxylate + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyoxylate reductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 334 amino acids
Theoretical weight: 38.06 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58320 (Residues: 1-334; Coverage: 100%)
Gene names: PH0597, gyaR
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 6 x NAP
1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P1
Unit cell:
a: 68.052Å b: 85.443Å c: 107.132Å
α: 113.76° β: 91.17° γ: 94°
R-values:
R R work R free
0.218 0.218 0.284
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Genetically encoded fluorescent sensors reveal dynamic regulation of NADPH metabolism.
Tao et al. (2017)
6 more

1 mention without citation

New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases.
Lassalle et al. (2016)