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The crystal structure of an alpha-(1-3,4)-fucosidase from bifidobacterium longum subsp. infantis atcc 15697

Analyse The crystal structure of an alpha-(1-3,4)-fucosidase from bifidobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MO4
Type
protein
Length
914 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-1,3/4-fucosidase
UniProt
B7GNN8
Ligands
TYR
Pockets
12 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-1,3/4-fucosidaseprotein45530% helix, 26% strandB7GNN8
BAlpha-1,3/4-fucosidaseprotein45930% helix, 26% strandB7GNN8

Ligands and binding sites

  • TYR · Tyrosine · ligand · chains A
  • FMT · Formic acid · additive · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15210.730.8241empty
21770.550.8036empty
31060.520.8325empty
41760.500.7727TYR
51760.480.7621empty

Interfaces

1 interface between chains.

  • A–B · 1380 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 17 modified (engineered).

Compared structures

  • 3MO4 · The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp.… · the same entry in another collection · chain A against A, TM-score 1.00

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