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Crystal structure of glucosyl-3-phosphoglycerate synthase from mycobacterium tuberculosis in complex with MG2+ and uridine- diphosphate (udp)

Analyse Crystal structure of glucosyl-3-phosphoglycerate synthase from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4DE7
Type
protein
Length
281 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucosyl-3-phosphoglycerate synthase (gpgs)
EC
2.4.1.-
UniProt
O05309
Ligands
UDP
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucosyl-3-phosphoglycerate synthase (gpgs) (EC 2.4.1.-)protein28140% helix, 19% strandO05309

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14310.730.8352UDP, GOL

Compared structures

  • 4DE7 · Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis… · the same entry in another collection · chain A against A, TM-score 1.00

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