Crystal structure of human tyrosylprotein sulfotransferase-1 complexed with PAP and C4 peptide. Determined by X-ray diffraction at 1.6 Å resolution. Released 13 Sept 2017.
Explore 5WRI in 3D Show helices and sheets RCSB PDB PDBe
5WRI contains 33 α-helices and 18 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-75 | 5 | 1 |
| α-helix | 82-90 | 9 | |
| β-strand | 95-96 | 2 | 1 |
| α-helix | 103-115 | 13 | |
| α-helix | 118-126 | 9 | |
| α-helix | 131-148 | 18 | |
| β-strand | 155-159 | 5 | 1 |
| α-helix | 161-166 | 6 | |
| α-helix | 167-173 | 7 | |
| β-strand | 177-183 | 7 | 1 |
| α-helix | 186-196 | 11 | |
| β-strand | 200-201 | 2 | 2 |
| α-helix | 208-229 | 22 | |
| β-strand | 234-238 | 5 | 1 |
| α-helix | 239-244 | 6 | |
| α-helix | 246-257 | 12 | |
| α-helix | 263-271 | 9 | |
| β-strand | 272 | 1 | 3 |
| β-strand | 278 | 1 | 3 |
| α-helix | 287-290 | 4 | |
| α-helix | 293 | 1 | |
| α-helix | 308-312 | 5 | |
| α-helix | 314-317 | 4 | |
| α-helix | 320-323 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-75 | 5 | 4 |
| α-helix | 82-90 | 9 | |
| β-strand | 95-96 | 2 | 4 |
| α-helix | 103-116 | 14 | |
| α-helix | 118-126 | 9 | |
| α-helix | 131-148 | 18 | |
| β-strand | 155-159 | 5 | 4 |
| α-helix | 161-166 | 6 | |
| α-helix | 167-173 | 7 | |
| β-strand | 177-183 | 7 | 4 |
| α-helix | 186-196 | 11 | |
| β-strand | 200-201 | 2 | 5 |
| α-helix | 208-229 | 22 | |
| β-strand | 234-238 | 5 | 4 |
| α-helix | 239-244 | 6 | |
| α-helix | 246-257 | 12 | |
| α-helix | 263-266 | 4 | |
| α-helix | 268-271 | 4 | |
| β-strand | 272 | 1 | 6 |
| β-strand | 278 | 1 | 6 |
| α-helix | 287-290 | 4 | |
| α-helix | 293 | 1 | |
| α-helix | 308-312 | 5 | |
| α-helix | 314-317 | 4 | |
| α-helix | 320-323 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1006-1007 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein-tyrosine sulfotransferase 1 | A, B | protein | 320 | Homo sapiens | O60507 (AlphaFold model) |
| Asp-phe-glu-asp-tyr-glu-phe-asp | D, E | protein | 8 | synthetic construct |
>5WRI_1 Protein-tyrosine sulfotransferase 1 (chains A, B) MGSSHHHHHHSSGLVPRGSHMKLESTRTTVRTGLDLKANKTFAYHKDMPLIFIGGVPRSG TTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAF LLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFLLMVRDGRASVHSMISRKVTIA GFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLQIPW NHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPML AKLGYDPYANPPNYGKPDPK
>5WRI_2 ASP-PHE-GLU-ASP-TYR-GLU-PHE-ASP (chains D, E) DFEDYEFD
Water and common crystallization additives (GOL) are not listed.
Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1. Tanaka, S., Nishiyori, T., Kojo, H. et al. Sci Rep (2017) 7:8776-8776. DOI 10.1038/s41598-017-07141-8 · PubMed
Other PDB entries of the same protein (UniProt O60507 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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