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Aspergillus kawachii beta-fructofuranosidase

Analyse Aspergillus kawachii beta-fructofuranosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XH9
Type
protein
Length
604 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Extracellular invertase
UniProt
G7XM46
Ligands
NA
Pockets
5 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AExtracellular invertaseprotein6047% helix, 45% strandG7XM46

Ligands and binding sites

  • NA · Sodium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14110.670.8032empty
21870.510.7726empty
31070.380.7529empty
4760.330.7523empty
5580.310.7610empty

Compared structures

  • 5XH9 · Aspergillus kawachii beta-fructofuranosidase · the same entry in another collection · chain A against A, TM-score 1.00

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