Gs-alpha complexed with GTP-gamma-S. Determined by X-ray diffraction at 2.3 Å resolution. Released 25 Feb 1998.
Explore 1AZT in 3D Show helices and sheets RCSB PDB PDBe
1AZT contains 43 α-helices and 16 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 | 36-39 | 4 | |
| β-strand | 41-46 | 6 | 1 |
| α-helix | 53-64 | 12 | |
| α-helix | 89-110 | 22 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 144-155 | 12 | |
| α-helix | 157-164 | 8 | |
| α-helix | 166-168 | 3 | |
| α-helix | 175-179 | 5 | |
| α-helix | 182-186 | 5 | |
| α-helix | 194-199 | 6 | |
| β-strand | 208-214 | 7 | 1 |
| β-strand | 217-223 | 7 | 1 |
| α-helix | 233-237 | 5 | |
| β-strand | 243-249 | 7 | 1 |
| α-helix | 252-254 | 3 | |
| β-strand | 256 | 1 | 2 |
| β-strand | 264 | 1 | 2 |
| α-helix | 265-277 | 13 | |
| α-helix | 280-282 | 3 | |
| β-strand | 286-292 | 7 | 1 |
| α-helix | 294-303 | 10 | |
| α-helix | 308-311 | 4 | |
| α-helix | 313-317 | 5 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-349 | 18 | |
| β-strand | 359-363 | 5 | 1 |
| α-helix | 369-377 | 9 | |
| α-helix | 380-388 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-39 | 4 | |
| β-strand | 41-46 | 6 | 3 |
| α-helix | 53-64 | 12 | |
| α-helix | 88-112 | 25 | |
| α-helix | 116-117 | 2 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 144-154 | 11 | |
| α-helix | 157-163 | 7 | |
| α-helix | 166-168 | 3 | |
| α-helix | 175-179 | 5 | |
| α-helix | 182-186 | 5 | |
| α-helix | 194-199 | 6 | |
| β-strand | 208-214 | 7 | 3 |
| β-strand | 217-223 | 7 | 3 |
| α-helix | 231-237 | 7 | |
| β-strand | 243-249 | 7 | 3 |
| α-helix | 250-254 | 5 | |
| β-strand | 256 | 1 | 4 |
| β-strand | 264 | 1 | 4 |
| α-helix | 265-277 | 13 | |
| α-helix | 280-282 | 3 | |
| β-strand | 287-292 | 6 | 3 |
| α-helix | 294-303 | 10 | |
| α-helix | 313-317 | 5 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-349 | 18 | |
| β-strand | 359-363 | 5 | 3 |
| α-helix | 369-389 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gs-alpha | A, B | protein | 402 | Bos taurus | P04896 (AlphaFold model) |
>1AZT_1 GS-ALPHA (chains A, B) MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELLGGHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| GSP | 5'-guanosine-diphosphate-monothiophosphate | C10 H16 N5 O13 P3 S | 2 |
| PO4 | Phosphate ion | O4 P | 16 |
| MG | Magnesium ion | Mg | 2 |
Crystal structure of the adenylyl cyclase activator Gsalpha. Sunahara, R.K., Tesmer, J.J., Gilman, A.G. et al. Science (1997) 278:1943-1947. DOI 10.1126/science.278.5345.1943 · PubMed
Other PDB entries of the same protein (UniProt P04896 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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