1omx

X-ray diffraction
2.4Å resolution

Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)

Released:

Function and Biology Details

Reaction catalysed:
UDP-N-acetyl-alpha-D-glucosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-190190 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exostosin-like 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 33.4 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ES89 (Residues: 38-330; Coverage: 89%)
Gene names: Extl2, Extr2
Sequence domains: Glycosyl transferase family 64 domain
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P4212
Unit cell:
a: 125.903Å b: 125.903Å c: 83.068Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.24
Expression system: Escherichia coli BL21(DE3)