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Crystal structure of ALPHA1,3-fucosyltransferase with GDP

Analyse Crystal structure of ALPHA1,3-fucosyltransferase with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NZX
Type
protein
Length
1,028 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ALPHA1,3-fucosyltransferase
EC
2.4.1.152
UniProt
O30511
Ligands
GDP, SO4
Pockets
11 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AALPHA1,3-fucosyltransferase (EC 2.4.1.152)protein34037% helix, 16% strandO30511
BALPHA1,3-fucosyltransferase (EC 2.4.1.152)protein33837% helix, 17% strandO30511
CALPHA1,3-fucosyltransferase (EC 2.4.1.152)protein35039% helix, 15% strandO30511

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
  • SO4 · Sulfate ion · ion · chains C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110150.790.80123empty
25410.710.8046empty
32800.580.7834empty
41740.550.8029empty
51470.520.8024empty

Interfaces

3 interfaces between chains.

  • A–C · 817 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 672 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 366 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2NZX · Crystal Structure of alpha1,3-Fucosyltransferase with GDP · the same entry in another collection · chain A against A, TM-score 1.00
  • O30511 · AlphaFold monomer V2.0 prediction for alpha-(1,3)-fucosyltransferase fuct (O30511) · a predicted model of the same protein · chain B against A, TM-score 0.99

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