1v83

X-ray diffraction
1.9Å resolution

Crystal structure of human GlcAT-P in complex with Udp and Mn2+

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 253 amino acids
Theoretical weight: 29.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P2W7 (Residues: 82-334; Coverage: 76%)
Gene names: B3GAT1, GLCATP
Sequence domains: Glycosyltransferase family 43
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 61.737Å b: 85.701Å c: 122.911Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.229
Expression system: Escherichia coli