Gtpase mechanism of gproteins from the 1.7-Å crystal structure of transducin alpha-GDP-ALF4-. Determined by X-ray diffraction at 1.7 Å resolution. Released 8 May 1995.
Explore 1TAD in 3D Show helices and sheets RCSB PDB PDBe
1TAD contains 60 α-helices and 25 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 28-35 | 8 | 1 |
| α-helix | 42-53 | 12 | |
| α-helix | 59-86 | 28 | |
| α-helix | 96-109 | 14 | |
| α-helix | 111 | 1 | |
| α-helix | 117-128 | 12 | |
| α-helix | 130-137 | 8 | |
| α-helix | 139-141 | 3 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-158 | 4 | |
| α-helix | 167-172 | 6 | |
| β-strand | 181-187 | 7 | 1 |
| β-strand | 190-196 | 7 | 1 |
| α-helix | 201-204 | 4 | |
| α-helix | 207-210 | 4 | |
| β-strand | 216-222 | 7 | 1 |
| α-helix | 223-227 | 5 | |
| β-strand | 229 | 1 | 2 |
| β-strand | 237 | 1 | 2 |
| α-helix | 238-250 | 13 | |
| α-helix | 253-255 | 3 | |
| β-strand | 259-265 | 7 | 1 |
| α-helix | 267-273 | 7 | |
| α-helix | 279-281 | 3 | |
| α-helix | 292-304 | 13 | |
| β-strand | 316-319 | 4 | 1 |
| α-helix | 325-341 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-36 | 8 | 3 |
| α-helix | 42-53 | 12 | |
| α-helix | 59-86 | 28 | |
| α-helix | 89-91 | 3 | |
| α-helix | 96-109 | 14 | |
| α-helix | 111 | 1 | |
| α-helix | 117-128 | 12 | |
| α-helix | 130-136 | 7 | |
| α-helix | 139-141 | 3 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-158 | 4 | |
| α-helix | 167-172 | 6 | |
| β-strand | 181-187 | 7 | 3 |
| β-strand | 190-196 | 7 | 3 |
| α-helix | 201-204 | 4 | |
| α-helix | 207-210 | 4 | |
| β-strand | 216-222 | 7 | 3 |
| α-helix | 223-227 | 5 | |
| β-strand | 229 | 1 | 4 |
| β-strand | 237 | 1 | 4 |
| α-helix | 238-250 | 13 | |
| α-helix | 253-255 | 3 | |
| β-strand | 259-265 | 7 | 3 |
| α-helix | 267-273 | 7 | |
| α-helix | 279-281 | 3 | |
| α-helix | 292-304 | 13 | |
| α-helix | 314-315 | 2 | |
| β-strand | 316-319 | 4 | 3 |
| α-helix | 325-341 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28-35 | 8 | 5 |
| α-helix | 42-53 | 12 | |
| α-helix | 59-63 | 5 | |
| α-helix | 65-86 | 22 | |
| α-helix | 95-107 | 13 | |
| α-helix | 111 | 1 | |
| α-helix | 117-127 | 11 | |
| α-helix | 130-137 | 8 | |
| α-helix | 139-141 | 3 | |
| α-helix | 148-153 | 6 | |
| α-helix | 155-159 | 5 | |
| β-strand | 163 | 1 | 1 |
| α-helix | 167-172 | 6 | |
| β-strand | 181-187 | 7 | 5 |
| β-strand | 190-196 | 7 | 5 |
| α-helix | 201-204 | 4 | |
| α-helix | 205-210 | 6 | |
| β-strand | 216-222 | 7 | 5 |
| α-helix | 223-227 | 5 | |
| β-strand | 229 | 1 | 6 |
| β-strand | 237 | 1 | 6 |
| α-helix | 238-250 | 13 | |
| α-helix | 253-255 | 3 | |
| β-strand | 259-265 | 7 | 5 |
| α-helix | 267-273 | 7 | |
| α-helix | 279-281 | 3 | |
| α-helix | 292-304 | 13 | |
| β-strand | 316-319 | 4 | 5 |
| α-helix | 325-342 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transducin-alpha | A, B, C | protein | 324 | Bos taurus | P04695 (AlphaFold model) |
>1TAD_1 TRANSDUCIN-ALPHA (chains A, B, C) ARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTT LNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLND SAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKK WIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNK KDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQ NVKFVFDAVTDIIIKENLKDCGLF
| ID | Name | Formula | Copies |
|---|---|---|---|
| CAC | Cacodylate ion | C2 H6 As O2 | 6 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 3 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 3 |
| CA | Calcium ion | Ca | 3 |
GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4. Sondek, J., Lambright, D.G., Noel, J.P. et al. Nature (1994) 372:276-279. DOI 10.1038/372276a0 · PubMed
Other PDB entries of the same protein (UniProt P04695 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1TAD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.