crystal structure of the GAP domain of MgcRacGAP(S387A). Determined by X-ray diffraction at 1.84 Å resolution. Released 21 Jan 2015.
Explore 3WPQ in 3D Show helices and sheets RCSB PDB PDBe
3WPQ contains 27 α-helices and 0 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 | 351-354 | 4 | |
| α-helix | 364-376 | 13 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-397 | 8 | |
| α-helix | 398-402 | 5 | |
| α-helix | 409-411 | 3 | |
| α-helix | 415-427 | 13 | |
| α-helix | 439-447 | 9 | |
| α-helix | 451-462 | 12 | |
| α-helix | 467-485 | 19 | |
| α-helix | 493-500 | 8 | |
| α-helix | 501-505 | 5 | |
| α-helix | 514-532 | 19 | |
| α-helix | 536-540 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 351-354 | 4 | |
| α-helix | 364-376 | 13 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-403 | 14 | |
| α-helix | 409-411 | 3 | |
| α-helix | 415-427 | 13 | |
| α-helix | 439-447 | 9 | |
| α-helix | 451-463 | 13 | |
| α-helix | 467-485 | 19 | |
| α-helix | 493-500 | 8 | |
| α-helix | 501-505 | 5 | |
| α-helix | 514-533 | 20 | |
| α-helix | 536-540 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rac GTPase-activating protein 1 | A, B | protein | 208 | Homo sapiens | Q9H0H5 (AlphaFold model) |
>3WPQ_1 Rac GTPase-activating protein 1 (chains A, B) GSSGSSGIGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRIAGCDRTVKELKE KFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAM YQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIVAHAVPNPDPVTMS QDIKRQPKVVERLLSLPLEYWSQFMMVE
Structural basis for the effects of Ser387 phosphorylation of MgcRacGAP on its GTPase-activating activities for CDC42 and RHOA. Murayama, K., Kato-Murayama, M., Hosaka, T. et al. J Struct Biol (2024) 216:108151-108151. DOI 10.1016/j.jsb.2024.108151 · PubMed
Other PDB entries of the same protein (UniProt Q9H0H5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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