2d0j

X-ray diffraction
2Å resolution

Crystal Structure of Human GlcAT-S Apo Form

Released:
Source organism: Homo sapiens
Entry authors: Shiba T, Kakuda S, Ishiguro M, Oka S, Kawasaki T, Wakatsuki S, Kato R

Function and Biology Details

Reaction catalysed:
UDP-alpha-D-glucuronate + [protein]-3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-serine = UDP + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 246 amino acids
Theoretical weight: 28.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NPZ5 (Residues: 78-323; Coverage: 76%)
Gene names: B3GAT2, GLCATS, KIAA1963
Sequence domains: Glycosyltransferase family 43
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 110.402Å b: 122.591Å c: 92.985Å
α: 90° β: 108.2° γ: 90°
R-values:
R R work R free
0.24 0.238 0.278
Expression system: Escherichia coli