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Mouse POFUT1 in complex with O-glucosylated EGF(+) and GDP

Analyse Mouse POFUT1 in complex with O-glucosylated EGF(+) and GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KY7
Type
protein
Length
385 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GDP-fucose protein O-fucosyltransferase 1; EGF(+)
EC
2.4.1.221
UniProt
Q91ZW2
Ligands
GDP, NAG, BGC
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221)protein34743% helix, 16% strandQ91ZW2
BEGF(+)protein3811% helix, 32% strand—

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • BGC · beta-D-glucopyranose · sugar · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14830.730.8242GDP
22070.560.7939empty

Interfaces

1 interface between chains.

  • A–B · 882 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide, 3 glycan (disulfide, N-glycosylation, O-glycosylation).

Compared structures

  • 5KY7 · mouse POFUT1 in complex with O-glucosylated EGF(+) and GDP · the same entry in another collection · chain A against A, TM-score 1.00
  • Q91ZW2 · AlphaFold monomer V2.0 prediction for GDP-fucose protein O-fucosyltransferase 1 (Q91ZW2) · a predicted model of the same protein · chain A against A, TM-score 0.99

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