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Co-structure of homo sapiens glycerol-3-phosphate dehydrogenase 1 complex with NAD

Analyse Co-structure of homo sapiens glycerol-3-phosphate dehydrogenase 1 complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1X0X
Type
protein
Length
350 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
EC
1.1.1.8
UniProt
P21695
Ligands
NAD, SO4
Pockets
1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic (EC 1.1.1.8)protein35053% helix, 14% strandP21695

Ligands and binding sites

  • NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
  • SO4 · Sulfate ion · ion · 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
13730.780.8847SO4, NAD

Compared structures

  • 1X0X · Co-Structure of Homo Sapiens Glycerol-3-Phosphate Dehydrogenase 1 complex with NAD · the same entry in another collection · chain A against A, TM-score 1.00
  • P21695 · AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(+)]… · a predicted model of the same protein · chain A against A, TM-score 0.98

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