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Impase (AF2372) R92Q/K164E

Analyse Impase (AF2372) R92Q/K164E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6B65
Type
protein
Length
504 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase
EC
3.1.3.11, 3.1.3.25
UniProt
O30298
Ligands
MG, SO4
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BFructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase (EC 3.1.3.11, 3.1.3.25)protein25230% helix, 29% strandO30298

Ligands and binding sites

  • MG · Magnesium ion · metal · 4 copies · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A, B
  • PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
  • IPA · Isopropyl alcohol · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14090.660.7942SO4, MG, IPA
23360.660.8133SO4, MG, IPA
3780.330.7416empty
4570.240.7212PEG

Interfaces

1 interface between chains.

  • A–B · 1178 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6B65 · IMPase (AF2372) R92Q/K164E · the same entry in another collection · chain A against A, TM-score 1.00
  • O30298 · AlphaFold monomer V2.0 prediction for fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphata… · a predicted model of the same protein · chain A against A, TM-score 1.00

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