› 4ap5

X-ray diffraction
3Å resolution

Crystal structure of human POFUT2

Released:
DOI: 10.2210/pdb4ap5/pdb
PDB entry 4ap5 coloured by chain, front view.
PDB entry 4ap5 coloured by chain, side view.
PDB entry 4ap5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.
Chen CI, Keusch JJ, Klein D, Hess D, Hofsteenge J, Gut H
EMBO J 31 3183-97 (2012)
PMID: 22588082

Function and Biology Details

Reaction catalysed: 
GDP-beta-L-fucose + [protein]-(L-serine/L-threonine) = GDP + [protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195130 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-fucose protein O-fucosyltransferase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 408 amino acids
Theoretical weight: 47.88 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9Y2G5 (Residues: 22-429; Coverage: 100%)
Gene names: C21orf80, FUT13, KIAA0958, POFUT2
Sequence domains: GDP-fucose protein O-fucosyltransferase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAG 4 x NAG
Ligand CL 1 x CL
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 118.628Å b: 118.628Å c: 196.227Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.174 0.236
Expression system: Homo sapiens

Quick links

Citations

7 review citations

Advances in understanding glycosyltransferases from a structural perspective.
Gloster TM. (2014)
6 more

6 mentions without citation

A perspective on structural and mechanistic aspects of protein O-fucosylation.
Lira-Navarrete et al. (2018)
5 more