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Crystal structure of human 4-hydroxy-2-oxoglutarate aldolase

Analyse Crystal structure of human 4-hydroxy-2-oxoglutarate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S5N
Type
protein
Length
295 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
4-hydroxy-2-oxoglutarate aldolase, mitochondrial
EC
4.1.3.16
UniProt
Q86XE5
Ligands
K, NA
Pockets
1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A4-hydroxy-2-oxoglutarate aldolase, mitochondrial (EC 4.1.3.16)protein29552% helix, 13% strandQ86XE5

Ligands and binding sites

  • K · Potassium ion · metal · chains A
  • NA · Sodium ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · 6 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
12900.570.7743EDO

Compared structures

  • 3S5N · Crystal Structure of Human 4-hydroxy-2-oxoglutarate Aldolase · the same entry in another collection · chain A against A, TM-score 1.00
  • Q86XE5 · AlphaFold monomer V2.0 prediction for 4-hydroxy-2-oxoglutarate aldolase, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 1.00

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