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The 1.55 a crystal structure of glycerol-3-phosphate acyltransferase

Analyse The 1.55 a crystal structure of glycerol-3-phosphate acyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1IUQ
Type
protein
Length
357 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycerol-3-phosphate acyltransferase
EC
2.3.1.15
UniProt
P10349
Ligands
SO4
Pockets
2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycerol-3-phosphate acyltransferase (EC 2.3.1.15)protein35752% helix, 12% strandP10349

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A
  • GOL · Glycerol · additive · 6 copies · 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
15620.800.8562SO4, GOL
2780.360.7617empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

  • 1IUQ · The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
  • P10349 · AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase ATS12… · a predicted model of the same protein · chain A against A, TM-score 0.99

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