Catalytic domain of human SHP2. Determined by X-ray diffraction at 1.4 Å resolution. Released 23 Apr 2014.
Explore 3ZM1 in 3D Show helices and sheets RCSB PDB PDBe
3ZM1 contains 14 α-helices and 11 β-strands across 1 chain. 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 | 251-253 | 3 | |
| α-helix | 266-269 | 4 | |
| α-helix | 271-276 | 6 | |
| α-helix | 286-288 | 3 | |
| β-strand | 289-291 | 3 | 1 |
| α-helix | 292 | 1 | |
| β-strand | 304-310 | 7 | 1 |
| β-strand | 327-331 | 5 | 1 |
| α-helix | 332-334 | 3 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| β-strand | 352-355 | 4 | 1 |
| β-strand | 360-361 | 2 | 2 |
| β-strand | 364-365 | 2 | 2 |
| α-helix | 372-373 | 2 | |
| β-strand | 376-380 | 5 | 1 |
| β-strand | 383-392 | 10 | 1 |
| β-strand | 396-405 | 10 | 1 |
| β-strand | 413-420 | 8 | 1 |
| α-helix | 433-447 | 15 | |
| α-helix | 454 | 1 | |
| β-strand | 455-459 | 5 | 1 |
| α-helix | 464-482 | 19 | |
| α-helix | 490-498 | 9 | |
| α-helix | 508-524 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tyrosine-protein phosphatase non-receptor type 11 | A | protein | 284 | HOMO SAPIENS | Q06124 (AlphaFold model) |
>3ZM1_1 TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11 (chains A) GAHMWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSD YINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERG KSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTW PDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKG VDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQR
Selective Inhibitors of the Protein Tyrosine Phosphatase Shp2 Block Cellular Motility and Growth of Cancer Cells in Vitro and in Vivo. Grosskopf, S., Eckert, C., Arkona, C. et al. ChemMedChem (2015) 10:815. DOI 10.1002/CMDC.201500015 · PubMed
Other PDB entries of the same protein (UniProt Q06124 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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