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Crystal structure of N1051A mutant of formylglycinamidine synthetase

Analyse Crystal structure of N1051A mutant of formylglycinamidine synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DW7
Type
protein
Length
1,290 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphoribosylformylglycinamidine synthase
EC
6.3.5.3
UniProt
A0A0D6F9Y3
Ligands
ADP, MG, SO4
Pockets
10 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphoribosylformylglycinamidine synthase (EC 6.3.5.3)protein129035% helix, 27% strandA0A0D6F9Y3

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · 3 copies · chains A
  • SO4 · Sulfate ion · ion · 19 copies · chains A
  • GOL · Glycerol · additive · 40 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
12970.860.9748ADP, MG
29920.830.8494GOL, SO4
39960.800.8183GOL, SO4
42630.790.9238GOL
51030.760.9732GOL

Compared structures

  • 7DW7 · Crystal Structure of N1051A mutant of Formylglycinamidine Synthetase · the same entry in another collection · chain A against A, TM-score 1.00

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