› 5kxq

X-ray diffraction
1.9Å resolution

mouse POFUT1 in complex with GDP

Released:
DOI: 10.2210/pdb5kxq/pdb
PDB entry 5kxq coloured by chain, front view.
PDB entry 5kxq coloured by chain, side view.
PDB entry 5kxq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.
Li Z, Han K, Pak JE, Satkunarajah M, Zhou D, Rini JM
Nat Chem Biol 13 757-763 (2017)
PMID: 28530709

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-187630 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-fucose protein O-fucosyltransferase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 354 amino acids
Theoretical weight: 40.45 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q91ZW2 (Residues: 32-385; Coverage: 98%)
Gene name: Pofut1
Sequence domains: GDP-fucose protein O-fucosyltransferase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAG 8 x NAG
Ligand GDP 4 x GDP
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 56.14Å b: 251.82Å c: 56.08Å
α: 90° β: 95.81° γ: 90°
R-values:
R R work R free
0.163 0.162 0.191
Expression system: Homo sapiens

Quick links

Citations

8 review citations

Protein O-fucosylation: structure and function.
Holdener et al. (2019)
7 more

1 mention without citation

Structural basis of substrate recognition and catalysis by fucosyltransferase 8.
Järvå et al. (2020)