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Adenylosuccinate synthetase in complex with the natural feedback inhibitor AMP

Analyse Adenylosuccinate synthetase in complex with the natural feedback inhibitor AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SON
Type
protein
Length
431 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Adenylosuccinate synthetase
EC
6.3.4.4
UniProt
P0A7D4
Ligands
AMP
Pockets
2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAdenylosuccinate synthetase (EC 6.3.4.4)protein43139% helix, 20% strandP0A7D4

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains A
  • BME · Beta-mercaptoethanol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16850.780.8364AMP
2810.390.7716empty

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

  • 1SON · Adenylosuccinate synthetase in complex with the natural feedback inhibitor AMP · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A7D4 · AlphaFold monomer V2.0 prediction for adenylosuccinate synthetase (P0A7D4) · a predicted model of the same protein · chain A against A, TM-score 0.99

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