Gi-alpha-1 bound to GDP and magnesium. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Jan 1999.
Explore 1BOF in 3D Show helices and sheets RCSB PDB PDBe
1BOF contains 22 α-helices and 7 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 | 11-16 | 6 | |
| α-helix | 20-23 | 4 | |
| α-helix | 27-29 | 3 | |
| α-helix | 30-31 | 2 | |
| β-strand | 32-40 | 9 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-67 | 5 | |
| α-helix | 70-91 | 22 | |
| α-helix | 100-111 | 12 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-140 | 7 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-163 | 5 | |
| α-helix | 171-175 | 5 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-231 | 5 | |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 1 |
| α-helix | 271-277 | 7 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 329-347 | 19 | |
| α-helix | 348-350 | 3 | |
| β-strand | 353 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gi alpha 1 | A | protein | 353 | Rattus norvegicus | P10824 (AlphaFold model) |
>1BOF_1 GI ALPHA 1 (chains A) GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGY SEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTA ELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKT TGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN RMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAA YIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Water and common crystallization additives (SO4) are not listed.
Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment. Coleman, D.E., Sprang, S.R. Biochemistry (1998) 37:14376-14385. DOI 10.1021/bi9810306 · PubMed
Other PDB entries of the same protein (UniProt P10824 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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