Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1. Determined by X-ray diffraction at 3.2 Å resolution. Released 3 Jun 2026.
Explore 9WP1 in 3D Show helices and sheets RCSB PDB PDBe
9WP1 contains 128 α-helices and 72 β-strands across 16 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 | 1 | 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 | 293-294 | 2 | |
| α-helix | 308-312 | 5 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-323 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-76 | 6 | 4 |
| α-helix | 82-90 | 9 | |
| β-strand | 95-96 | 2 | 4 |
| α-helix | 103-115 | 13 | |
| 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 | 1 | 5 |
| α-helix | 208-229 | 22 | |
| β-strand | 234-238 | 5 | 4 |
| α-helix | 239-244 | 6 | |
| α-helix | 246-257 | 12 | |
| α-helix | 263-271 | 9 | |
| β-strand | 272 | 1 | 6 |
| β-strand | 278 | 1 | 6 |
| α-helix | 287-290 | 4 | |
| α-helix | 293-294 | 2 | |
| α-helix | 308-312 | 5 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-323 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-75 | 5 | 19 |
| α-helix | 82-90 | 9 | |
| β-strand | 95-96 | 2 | 19 |
| α-helix | 103-115 | 13 | |
| α-helix | 118-126 | 9 | |
| α-helix | 131-148 | 18 | |
| β-strand | 155-159 | 5 | 19 |
| α-helix | 161-166 | 6 | |
| α-helix | 167-173 | 7 | |
| β-strand | 177-183 | 7 | 19 |
| α-helix | 186-196 | 11 | |
| β-strand | 200 | 1 | 20 |
| α-helix | 208-229 | 22 | |
| β-strand | 234-238 | 5 | 19 |
| α-helix | 239-244 | 6 | |
| α-helix | 246-257 | 12 | |
| α-helix | 263-271 | 9 | |
| β-strand | 272 | 1 | 21 |
| β-strand | 278 | 1 | 21 |
| α-helix | 287-290 | 4 | |
| α-helix | 293 | 1 | |
| α-helix | 308-312 | 5 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-323 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein-tyrosine sulfotransferase 1 | A, B, C, D, E, F, G, H | protein | 276 | Homo sapiens | O60507 (AlphaFold model) |
| C-C chemokine receptor type 5 | L, M, N, O, P, Q, R, S | protein | 6 | Homo sapiens | P51681 (AlphaFold model) |
>9WP1_1 Protein-tyrosine sulfotransferase 1 (chains A, B, C, D, E, F, G, H) AYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIR LDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFLLMV RDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLV LHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWV GKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPD
>9WP1_2 C-C chemokine receptor type 5 (chains L, M, N, O, P, Q, R, S) MDYQVS
Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1. Tanaka, S., Asano, H., Toyoda, K. et al. FEBS J (2026). DOI 10.1111/febs.70597 · 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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