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Crystal structure of a glucose-6-phosphate isomerase from chlamydia trachomatis D/UW-3/CX

Analyse Crystal structure of a glucose-6-phosphate isomerase from chlamydia trachomatis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OTU
Type
protein
Length
517 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucose-6-phosphate isomerase
EC
5.3.1.9
UniProt
A0A0E9E8R5
Ligands
G6Q
Pockets
3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucose-6-phosphate isomerase (EC 5.3.1.9)protein51751% helix, 14% strandA0A0E9E8R5

Ligands and binding sites

  • G6Q · Glucose-6-phosphate · ligand · chains A
  • ACT · Acetate ion · additive · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12470.610.8138G6Q
21530.480.7725empty
3570.330.7714empty

Compared structures

  • 6OTU · Crystal structure of a glucose-6-phosphate isomerase from Chlamydia trachomatis D/UW-3/Cx · the same entry in another collection · chain A against A, TM-score 1.00

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