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Glutamate dehydrogenase from thermococcus litoralis

Analyse Glutamate dehydrogenase from thermococcus litoralis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BVU
Type
protein
Length
2,496 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (glutamate dehydrogenase)
EC
1.4.1.3
UniProt
Q56304
Pockets
20 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FProtein (glutamate dehydrogenase) (EC 1.4.1.3)protein41650% helix, 16% strandQ56304

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111380.890.91124empty
28160.890.9259empty
38290.890.9258empty
48930.740.7875empty
57600.740.7958empty

Interfaces

15 interfaces between chains.

  • B–E · 1058 Ų buried · 10 hydrogen bonds · protein-protein
  • A–F · 1056 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1051 Ų buried · 12 hydrogen bonds · protein-protein
  • E–F · 968 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 949 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 1BVU · Glutamate dehydrogenase from thermococcus litoralis · the same entry in another collection · chain A against A, TM-score 1.00
  • Q56304 · AlphaFold monomer V2.0 prediction for glutamate dehydrogenase (Q56304) · a predicted model of the same protein · chain A against A, TM-score 0.99

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