Crystal structure of SHP1 catalytic domain with JAK1 activation loop peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 19 Dec 2012.
Explore 4GS0 in 3D Show helices and sheets RCSB PDB PDBe
4GS0 contains 28 α-helices and 22 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 244-257 | 14 | |
| α-helix | 258-260 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 268-273 | 6 | |
| α-helix | 283-285 | 3 | |
| β-strand | 286 | 1 | 1 |
| α-helix | 287-289 | 3 | |
| β-strand | 304-307 | 4 | 1 |
| β-strand | 321-324 | 4 | 1 |
| α-helix | 325-328 | 4 | |
| α-helix | 329-331 | 3 | |
| α-helix | 332-342 | 11 | |
| β-strand | 346-349 | 4 | 1 |
| β-strand | 354-355 | 2 | 2 |
| β-strand | 358-359 | 2 | 2 |
| α-helix | 366-367 | 2 | |
| β-strand | 371-374 | 4 | 1 |
| β-strand | 377-386 | 10 | 1 |
| β-strand | 390-399 | 10 | 1 |
| β-strand | 407-414 | 8 | 1 |
| α-helix | 427-441 | 15 | |
| α-helix | 448 | 1 | |
| β-strand | 449-452 | 4 | 1 |
| α-helix | 459-476 | 18 | |
| α-helix | 484-492 | 9 | |
| α-helix | 502-525 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 264-266 | 3 | |
| α-helix | 268-273 | 6 | |
| α-helix | 283-285 | 3 | |
| β-strand | 286-288 | 3 | 3 |
| α-helix | 289 | 1 | |
| β-strand | 301-307 | 7 | 3 |
| β-strand | 321-324 | 4 | 3 |
| α-helix | 325-328 | 4 | |
| α-helix | 329-331 | 3 | |
| α-helix | 332-342 | 11 | |
| β-strand | 346-349 | 4 | 3 |
| β-strand | 354-355 | 2 | 4 |
| β-strand | 358-359 | 2 | 4 |
| α-helix | 366-367 | 2 | |
| β-strand | 371-374 | 4 | 3 |
| β-strand | 377-386 | 10 | 3 |
| β-strand | 390-399 | 10 | 3 |
| β-strand | 407-414 | 8 | 3 |
| α-helix | 427-441 | 15 | |
| α-helix | 448 | 1 | |
| β-strand | 449-452 | 4 | 3 |
| α-helix | 459-476 | 18 | |
| α-helix | 484-492 | 9 | |
| α-helix | 502-522 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tyrosine-protein phosphatase non-receptor type 6 | A, B | protein | 308 | Homo sapiens | P29350 (AlphaFold model) |
| Tyrosine-protein kinase JAK1 | C | protein | 4 | Homo sapiens | P23458 (AlphaFold model) |
>4GS0_1 Tyrosine-protein phosphatase non-receptor type 6 (chains A, B) MHHHHHHGSLVPRSENLYFQGSGFWEEFESLQKQEVKNLHQRLEGQRPENKGKNRYKNIL PFDHSRVILQGRDSNIPGSDYINANYIKNQLLGPDENAKTYIASQGCLEATVNDFWQMAW QENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPL DNGDLIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRT GTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTK KKLEVLQS
>4GS0_2 Tyrosine-protein kinase JAK1 (chains C) XXYX
Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition. Alicea-Velazquez, N.L., Jakoncic, J., Boggon, T.J. J Struct Biol (2013) 181:243-251. DOI 10.1016/j.jsb.2012.12.009 · PubMed
Other PDB entries of the same protein (UniProt P29350 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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