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Crystal structure of human glycolate oxidase (go) in complex with cdst

Analyse Crystal structure of human glycolate oxidase (go) in complex with cdst in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RDT
Type
protein
Length
335 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydroxyacid oxidase 1
EC
1.1.3.15
UniProt
Q9UJM8
Ligands
FMN, 2RD
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHydroxyacid oxidase 1 (EC 1.1.3.15)protein33547% helix, 15% strandQ9UJM8

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · chains A
  • 2RD · 5-(dodecylthio)-1H-1,2,3-triazole-4-carboxylic acid · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12060.780.9238FMN, 2RD
2980.430.7820empty
3630.300.7414empty

Compared structures

  • 2RDT · Crystal Structure of Human Glycolate Oxidase (GO) in Complex with CDST · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UJM8 · AlphaFold monomer V2.0 prediction for hydroxyacid oxidase 1 (Q9UJM8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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