› 3ap3

X-ray diffraction
3.5Å resolution

Crystal structure of human tyrosylprotein sulfotransferase-2 complexed with PAP

Released:
DOI: 10.2210/pdb3ap3/pdb
PDB entry 3ap3 coloured by chain, front view.
PDB entry 3ap3 coloured by chain, side view.
PDB entry 3ap3 coloured by chain, top view.
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
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130074 (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

8 review citations

The Regulation of Steroid Action by Sulfation and Desulfation.
Mueller et al. (2015)
7 more

4 mentions without citation

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