Structures of active conformations of gi alpha 1 and the mechanism of GTP hydrolysis. Determined by X-ray diffraction at 2.2 Å resolution. Released 31 Mar 1995.
Explore 1GFI in 3D Show helices and sheets RCSB PDB PDBe
1GFI contains 18 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 | 34-39 | 6 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-68 | 6 | |
| α-helix | 70-90 | 21 | |
| α-helix | 100-115 | 16 | |
| α-helix | 121-131 | 11 | |
| α-helix | 134-140 | 7 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-162 | 4 | |
| α-helix | 171-175 | 5 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 205-214 | 10 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-229 | 3 | |
| β-strand | 233-234 | 2 | 2 |
| β-strand | 237-241 | 5 | 2 |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 1 |
| α-helix | 271-278 | 8 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 329-344 | 16 |
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Coleman, D.E., Berghuis, A.M., Lee, E. et al. Science (1994) 265:1405-1412. PubMed
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