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Crystal structure of levan fructotransferase D54N mutant from arthrobacter ureafaciens in complex with levanbiose

Analyse Crystal structure of levan fructotransferase D54N mutant from arthrobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4FFI
Type
protein
Length
1,917 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Levan fructotransferase
EC
4.2.2.16
UniProt
Q9KJD0
Ligands
FRU
Pockets
20 · best druggability 0.60

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLevan fructotransferase (EC 4.2.2.16)protein4807% helix, 49% strandQ9KJD0
CLevan fructotransferase (EC 4.2.2.16)protein4798% helix, 49% strandQ9KJD0
DLevan fructotransferase (EC 4.2.2.16)protein4788% helix, 50% strandQ9KJD0

Ligands and binding sites

  • FRU · beta-D-fructofuranose · sugar · 21 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12670.600.7933FRU
22760.600.7928empty
32900.590.7828empty
42480.590.7936FRU
52850.590.7826empty

Interfaces

4 interfaces between chains.

  • A–B · 423 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 313 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 277 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 43 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4FFI · Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in… · the same entry in another collection · chain A against A, TM-score 1.00

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