› 5bo6

X-ray diffraction
2.07Å resolution

Structure of human sialyltransferase ST8SiaIII in complex with CDP

Released:
DOI: 10.2210/pdb5bo6/pdb
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PDB entry 5bo6 coloured by chain, front view.
PDB entry 5bo6 coloured by chain, side view.
PDB entry 5bo6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation.
Volkers G, Worrall LJ, Kwan DH, Yu CC, Baumann L, Lameignere E, Wasney GA, Scott NE, Wakarchuk W, Foster LJ, Withers SG, Strynadka NC
Nat Struct Mol Biol 22 627-35 (2015)
PMID: 26192331

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128863 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-N-acetylneuraminate alpha-2,8-sialyltransferase ST8SIA3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 37.92 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O43173 (Residues: 81-380; Coverage: 79%)
Gene names: SIAT8C, ST8SIA3
Sequence domains: Glycosyltransferase family 29 (sialyltransferase)
Structure domains: Glycosyl transferase family 29

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
2 bound ligands:
Ligand CDP 2 x CDP
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P212121
Unit cell:
a: 72.928Å b: 96.867Å c: 124.981Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.202
Expression system: Spodoptera frugiperda

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Citations

12 review citations

Sialylation of N-glycans: mechanism, cellular compartmentalization and function.
Bhide et al. (2017)
11 more

6 mentions without citation

Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized.
Kellokumpu et al. (2016)
5 more

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