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Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate

Analyse Structural studies on the synchronization of catalytic centers in glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LLW
Type
protein
Length
1,475 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferredoxin-dependent glutamate synthase
EC
1.4.7.1
UniProt
P55038
Ligands
FMN, F3S, AKG
Pockets
19 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerredoxin-dependent glutamate synthase (EC 1.4.7.1)protein147536% helix, 17% strandP55038

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · chains A
  • F3S · FE3-S4 cluster · ligand · chains A
  • AKG · 2-oxoglutaric acid · ligand · chains A

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

Pockets

19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12310.840.9646empty
22500.830.9663FMN, F3S, AKG
35990.720.8072empty
41700.670.8738empty
53770.660.8056empty

Compared structures

  • 1LLW · Structural studies on the synchronization of catalytic centers in glutamate synthase… · the same entry in another collection · chain A against A, TM-score 1.00
  • P55038 · AlphaFold monomer V2.0 prediction for ferredoxin-dependent glutamate synthase 2 (P55038) · a predicted model of the same protein · chain A against A, TM-score 1.00

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