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Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE from thermoproteus neutrophilus, ligand free

Analyse Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE from thermoproteus neutrophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3T2B
Type
protein
Length
379 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE
EC
4.1.2.13, 3.1.3.11
UniProt
B1YAL1
Ligands
MG
Pockets
2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE (EC 4.1.2.13, 3.1.3.11)protein37931% helix, 29% strandB1YAL1

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13110.640.8034empty
2590.320.7617empty

Compared structures

  • 3T2B · Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, ligand… · the same entry in another collection · chain A against A, TM-score 1.00
  • B1YAL1 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE… · a predicted model of the same protein · chain A against A, TM-score 0.99

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