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Cryo-EM structure of glutamate dehydrogenase from thermococcus profundus

Analyse Cryo-EM structure of glutamate dehydrogenase from thermococcus profundus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JND
Type
protein
Length
419 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate dehydrogenase
EC
1.4.1.3
UniProt
O74024
Pockets
3 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 41% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate dehydrogenase (EC 1.4.1.3)protein41941% helix, 14% strandO74024

Ligands and binding sites

  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17140.750.8057TRS
2750.510.8514empty
3550.340.7814empty

Compared structures

  • 6JND · Cryo-EM structure of glutamate dehydrogenase from Thermococcus profundus · the same entry in another collection · chain A against A, TM-score 1.00
  • O74024 · AlphaFold monomer V2.0 prediction for glutamate dehydrogenase (O74024) · a predicted model of the same protein · chain A against A, TM-score 0.98

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