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Formylglycinamide ribonucleotide amidotransferase from salmonella typhimurium: role of the ATP complexation and glutaminase domain in catalytic coupling

Analyse Formylglycinamide ribonucleotide amidotransferase from salmonella typhimurium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UMM
Type
protein
Length
1,285 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphoribosylformylglycinamidine synthase
EC
6.3.5.3
UniProt
P74881
Ligands
ANP, ADP, MG, SO4
Pockets
10 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphoribosylformylglycinamidine synthase (EC 6.3.5.3)protein128533% helix, 27% strandP74881

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · 3 copies · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12900.860.9745ADP, MG
29830.830.8485SO4
31230.790.9834empty
42630.780.9035empty
59690.770.8086ANP, SO4

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 3UMM · Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: Role of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P74881 · AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine synthase (P74881) · a predicted model of the same protein · chain A against A, TM-score 0.99

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