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Neutral trehalase NTH1 from saccharomyces cerevisiae in complex with trehalose

Analyse Neutral trehalase NTH1 from saccharomyces cerevisiae in complex with trehalose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5M4A
Type
protein
Length
548 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Neutral trehalase
EC
3.2.1.28
UniProt
P32356
Ligands
GLC
Pockets
8 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANeutral trehalase (EC 3.2.1.28)protein54850% helix, 10% strandP32356

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12600.660.8225GLC
21630.490.7721empty
31190.450.7716empty
4600.410.8117empty
51260.410.7524empty

Compared structures

  • 5M4A · Neutral trehalase Nth1 from Saccharomyces cerevisiae in complex with trehalose · the same entry in another collection · chain A against A, TM-score 1.00
  • P32356 · AlphaFold monomer V2.0 prediction for neutral trehalase (P32356) · a predicted model of the same protein · chain A against A, TM-score 1.00

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