› 3ap3

X-ray diffraction
3.5Å resolution

Crystal structure of human tyrosylprotein sulfotransferase-2 complexed with PAP

Released:
DOI: 10.2210/pdb3ap3/pdb
PDB 3ap3 coloured by chain and viewed from the front.
PDB 3ap3 coloured by chain and viewed from the side.
PDB 3ap3 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction.
Teramoto T, Fujikawa Y, Kawaguchi Y, Kurogi K, Soejima M, Adachi R, Nakanishi Y, Mishiro-Sato E, Liu MC, Sakakibara Y, Suiko M, Kimura M, Kakuta Y
OpenAccess logo Nat Commun 4 1572 (2013)
PMID: 23481380

Function and Biology Details

Reaction catalysed: 
3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-tyrosine sulfotransferase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 355 amino acids
Theoretical weight: 39.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60704 (Residues: 43-377; Coverage: 89%)
Gene name: TPST2
Sequence domains: Sulfotransferase family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand A3P 4 x A3P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Unit cell:
a: 71.432Å b: 81.326Å c: 226.659Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.294 0.29 0.371
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Selectins-The Two Dr. Jekyll and Mr. Hyde Faces of Adhesion Molecules-A Review.
Tvaroška et al. (2020)
4 more

2 mentions without citation

Tyrosine sulfation as a protein post-translational modification.
Yang et al. (2015)
1 more