› 1vkj

X-ray diffraction
2.5Å resolution

Crystal structure of heparan sulfate 3-O-sulfotransferase isoform 1 in the presence of PAP

Released:
DOI: 10.2210/pdb1vkj/pdb
PDB entry 1vkj coloured by chain, front view.
PDB entry 1vkj coloured by chain, side view.
PDB entry 1vkj coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure and mutational analysis of heparan sulfate 3-O-sulfotransferase isoform 1.
Edavettal SC, Lee KA, Negishi M, Linhardt RJ, Liu J, Pedersen LC
J Biol Chem 279 25789-97 (2004)
PMID: 15060080

Function and Biology Details

Reaction catalysed: 
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heparan sulfate glucosamine 3-O-sulfotransferase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 285 amino acids
Theoretical weight: 33.26 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O35310 (Residues: 48-311; Coverage: 91%)
Gene names: 3ost, 3ost1, Hs3st1
Sequence domains: Sulfotransferase domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand A3P 3 x A3P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I4122
Unit cell:
a: 300.136Å b: 300.136Å c: 84.196Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 0.264
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Glycomics approach to structure-function relationships of glycosaminoglycans.
Sasisekharan et al. (2006)
13 more

4 mentions without citation

Heparan sulfate 3-O-sulfation: a rare modification in search of a function.
Thacker et al. (2014)
3 more