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Crystal structure of recombinant type I fructose-1,6-bisphosphatase from escherichia COLI complexed with sulfate ions

Analyse Crystal structure of recombinant type I fructose-1,6-bisphosphatase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GQ1
Type
protein
Length
310 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructose-1,6-bisphosphatase
EC
3.1.3.11
UniProt
P0A993
Ligands
SO4
Pockets
2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFructose-1,6-bisphosphatase (EC 3.1.3.11)protein31039% helix, 25% strandP0A993

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 7 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
11300.420.7622SO4
2960.400.7721empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 2GQ1 · Crystal Structure of Recombinant Type I Fructose-1,6-bisphosphatase from Escherichia coli… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A993 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase class 1 (P0A993) · a predicted model of the same protein · chain A against A, TM-score 0.99

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