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Crystal structure of putative beta-phosphoglucomutase from thermotoga maritima

Analyse Crystal structure of putative beta-phosphoglucomutase from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KBB
Type
protein
Length
216 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphorylated carbohydrates phosphatase TM_1254
EC
3.1.3.-
UniProt
Q9X0Y1
Ligands
SO4
Pockets
2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphorylated carbohydrates phosphatase TM_1254 (EC 3.1.3.-)protein21653% helix, 13% strandQ9X0Y1

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A
  • GOL · Glycerol · additive · 4 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11950.430.7329SO4
2770.390.7813empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 3KBB · Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9X0Y1 · AlphaFold monomer V2.0 prediction for phosphorylated carbohydrates phosphatase TM_1254… · a predicted model of the same protein · chain A against A, TM-score 0.95

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