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Crystal structure of glyoxylate reductase (PH0597) from pyrococcus horikoshii OT3, complexed with NADP (I41)

Analyse Crystal structure of glyoxylate reductase (PH0597) from pyrococcus horikoshii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2DBQ
Type
protein
Length
333 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glyoxylate reductase
EC
1.1.1.26
UniProt
O58320
Ligands
NAP, SO4
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlyoxylate reductase (EC 1.1.1.26)protein33339% helix, 15% strandO58320

Ligands and binding sites

  • NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · 5 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17120.720.7963SO4, NAP, GOL

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 2DBQ · Crystal Structure of Glyoxylate Reductase (PH0597) from Pyrococcus horikoshii OT3… · the same entry in another collection · chain A against A, TM-score 1.00
  • O58320 · AlphaFold monomer V2.0 prediction for glyoxylate reductase (O58320) · a predicted model of the same protein · chain A against A, TM-score 1.00

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