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Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/F447V/F470Y/P500S

Analyse Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WPV
Type
protein
Length
1,614 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-fructofuranosidase
EC
3.2.1.26
UniProt
Q8VW87
Pockets
20 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CBeta-fructofuranosidase (EC 3.2.1.26)protein53816% helix, 37% strandQ8VW87

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A, B, C

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

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15950.670.7752empty
24850.640.7741GOL
34310.630.7742GOL
43930.630.7850GOL
52150.550.7934empty

Interfaces

2 interfaces between chains.

  • A–B · 460 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 297 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3WPV · Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/F447V/F470Y/P500S · the same entry in another collection · chain A against A, TM-score 1.00

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