Crystal structure of RIT1 in the GDP state. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Sept 2025.
Explore 9MF1 in 3D Show helices and sheets RCSB PDB PDBe
9MF1 contains 6 α-helices and 8 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 |
|---|---|---|---|
| β-strand | 21-28 | 8 | 1 |
| α-helix | 34-43 | 10 | |
| β-strand | 56-64 | 9 | 1 |
| β-strand | 67-75 | 9 | 1 |
| α-helix | 84-92 | 9 | |
| β-strand | 95-101 | 7 | 1 |
| α-helix | 105-122 | 18 | |
| β-strand | 129-134 | 6 | 1 |
| α-helix | 139-141 | 3 | |
| α-helix | 146-156 | 11 | |
| β-strand | 160-162 | 3 | 1 |
| β-strand | 164 | 1 | 2 |
| β-strand | 169 | 1 | 2 |
| α-helix | 171-194 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding protein Rit1 | A | protein | 197 | Homo sapiens | Q92963 (AlphaFold model) |
>9MF1_1 GTP-binding protein Rit1 (chains A) GDSGTRPVGSCCSSPAGLSREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKI RIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYR VRRTDDTPVVLVGNKSDLKQLRQVTKEEGLALAREFSCPFFETSAAYRYYIDDVFHALVR EIRRKEKEAVLAMEKKS
Water and common crystallization additives (GOL) are not listed.
Structural basis for LZTR1 recognition of RAS GTPases for degradation. Dharmaiah, S., Bonsor, D.A., Mo, S.P. et al. Science (2025) 389:1112-1117. DOI 10.1126/science.adv7088 · PubMed
Other PDB entries of the same protein (UniProt Q92963 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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