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
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Alpha-(1,6)-fucosyltransferase (preferred)
PDBe Complex ID:
PDB-CPX-189827 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-(1,6)-fucosyltransferase
Molecule details ›
Chains: A, B, G, H
Length: 481 amino acids
Theoretical weight: 55.75 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains:
Length: 481 amino acids
Theoretical weight: 55.75 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
Q9BYC5 (Residues: 105-575; Coverage: 82%)
Sequence domains:
Ligands and Environments
No modified residues
Experiments and Validation Details
X-ray source:
AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup:
C2
Expression system: Spodoptera frugiperda
