› 6x5s

X-ray diffraction
3.3Å resolution

Human Alpha-1,6-fucosyltransferase (FUT8) bound to GDP and A3'-Asn

Released:
DOI: 10.2210/pdb6x5s/pdb
PDB entry 6x5s coloured by chain, front view.
PDB entry 6x5s coloured by chain, side view.
PDB entry 6x5s coloured by chain, top view.
Source organisms:
Primary publication:
Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases.
Boruah BM, Kadirvelraj R, Liu L, Ramiah A, Li C, Zong G, Bosman GP, Yang JY, Wang LX, Boons GJ, Wood ZA, Moremen KW
J Biol Chem 295 17027-17045 (2020)
PMID: 33004438

Function and Biology Details

Reaction catalysed: 
GDP-beta-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-167748 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Alpha-(1,6)-fucosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 466 amino acids
Theoretical weight: 53.78 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9BYC5 (Residues: 108-573; Coverage: 81%)
Gene name: FUT8
Sequence domains:
A3'-Asn Chains: C, D
Molecule details ›
Chains: C, D
Length: 3 amino acids
Theoretical weight: 332 Da
Source organism: Gallus gallus

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
3 bound ligands:
Ligand CL 13 x CL
Ligand GOL 1 x GOL
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6522
Unit cell:
a: 150.5Å b: 150.5Å c: 480.31Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.224
Expression system: Homo sapiens

Quick links

Citations

5 review citations

FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer.
Bastian et al. (2021)
4 more

1 mention without citation

Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases.
Boruah et al. (2020)