› 6x5u

X-ray diffraction
3.2Å resolution

Human Alpha-1,6-fucosyltransferase (FUT8) bound to GDP and NM5M2-Asn

Released:
DOI: 10.2210/pdb6x5u/pdb
PDB entry 6x5u coloured by chain, front view.
PDB entry 6x5u coloured by chain, side view.
PDB entry 6x5u coloured by chain, top view.
Source organism: Homo sapiens
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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189827 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (5 distinct):
Alpha-(1,6)-fucosyltransferase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 535 amino acids
Theoretical weight: 61.85 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9BYC5 (Residues: 41-575; Coverage: 93%)
Gene name: FUT8
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
2 bound ligands:
Ligand GDP 8 x GDP
Ligand ASN 2 x ASN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P65
Unit cell:
a: 154.02Å b: 154.02Å c: 466.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.19 0.236
Expression system: Homo sapiens

Quick links

Citations

7 review citations

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

1 mention without citation

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