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Glutamate dehydrogenase in complex with NADH, open conformation

Analyse Glutamate dehydrogenase in complex with NADH, open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3JD2
Type
protein
Length
2,976 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate dehydrogenase 1, mitochondrial
EC
1.4.1.3
UniProt
P00366
Ligands
NAI
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 46% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FGlutamate dehydrogenase 1, mitochondrial (EC 1.4.1.3)protein49646% helix, 13% strandP00366

Ligands and binding sites

  • NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 12 copies · chains A, B, C, D, E, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17580.860.8946empty
27110.850.8939empty
38600.840.8680NAI
48220.830.8677NAI
59400.830.8586NAI

Interfaces

15 interfaces between chains.

  • D–F · 1941 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 1940 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 1936 Ų buried · 12 hydrogen bonds · protein-protein
  • E–F · 1936 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 1933 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 3JD2 · Glutamate dehydrogenase in complex with NADH, open conformation · the same entry in another collection · chain F against F, TM-score 1.00
  • P00366 · AlphaFold monomer V2.0 prediction for glutamate dehydrogenase 1, mitochondrial (P00366) · a predicted model of the same protein · chain B against A, TM-score 0.91

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