The 2.2 Å crystal structure of transducin-alpha complexed with GTP gamma S. Determined by X-ray diffraction at 2.2 Å resolution. Released 31 Jul 1994.
Explore 1TND in 3D Show helices and sheets RCSB PDB PDBe
1TND contains 60 α-helices and 27 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 | 96-106 | 11 | |
| 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 | |
| β-strand | 163 | 1 | 2 |
| α-helix | 167-172 | 6 | |
| β-strand | 180-187 | 8 | 1 |
| β-strand | 190-197 | 8 | 1 |
| α-helix | 201-204 | 4 | |
| α-helix | 205-210 | 6 | |
| β-strand | 216-222 | 7 | 1 |
| α-helix | 223-227 | 5 | |
| β-strand | 229 | 1 | 3 |
| β-strand | 237 | 1 | 3 |
| α-helix | 238-250 | 13 | |
| α-helix | 254-256 | 3 | |
| β-strand | 259-265 | 7 | 1 |
| α-helix | 267-274 | 8 | |
| α-helix | 279-281 | 3 | |
| α-helix | 292-304 | 13 | |
| β-strand | 310 | 1 | 4 |
| β-strand | 313 | 1 | 4 |
| β-strand | 316-320 | 5 | 1 |
| α-helix | 325-341 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28-36 | 9 | 2 |
| α-helix | 42-53 | 12 | |
| α-helix | 59-63 | 5 | |
| α-helix | 66-87 | 22 | |
| α-helix | 94-96 | 3 | |
| α-helix | 97-107 | 11 | |
| α-helix | 111 | 1 | |
| α-helix | 117-128 | 12 | |
| α-helix | 132-137 | 6 | |
| α-helix | 139-141 | 3 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-159 | 5 | |
| α-helix | 167-171 | 5 | |
| β-strand | 180-186 | 7 | 2 |
| β-strand | 190-197 | 8 | 2 |
| α-helix | 201-204 | 4 | |
| α-helix | 205-210 | 6 | |
| β-strand | 216-222 | 7 | 2 |
| α-helix | 223-227 | 5 | |
| β-strand | 229 | 1 | 5 |
| β-strand | 237 | 1 | 5 |
| α-helix | 238-250 | 13 | |
| β-strand | 259-265 | 7 | 2 |
| α-helix | 267-276 | 10 | |
| α-helix | 279-281 | 3 | |
| α-helix | 292-304 | 13 | |
| α-helix | 308-311 | 4 | |
| β-strand | 317-320 | 4 | 2 |
| α-helix | 325-341 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-35 | 7 | 6 |
| α-helix | 42-53 | 12 | |
| α-helix | 59-64 | 6 | |
| α-helix | 66-87 | 22 | |
| α-helix | 96-107 | 12 | |
| α-helix | 111 | 1 | |
| α-helix | 117-127 | 11 | |
| α-helix | 130-136 | 7 | |
| α-helix | 139-141 | 3 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-159 | 5 | |
| α-helix | 167-172 | 6 | |
| β-strand | 180-187 | 8 | 6 |
| β-strand | 190-197 | 8 | 6 |
| α-helix | 201-204 | 4 | |
| α-helix | 207-210 | 4 | |
| β-strand | 216-222 | 7 | 6 |
| α-helix | 223-227 | 5 | |
| β-strand | 229 | 1 | 7 |
| β-strand | 237 | 1 | 7 |
| α-helix | 238-250 | 13 | |
| α-helix | 253-255 | 3 | |
| β-strand | 259-265 | 7 | 6 |
| α-helix | 267-273 | 7 | |
| α-helix | 279-281 | 3 | |
| α-helix | 292-304 | 13 | |
| β-strand | 316-319 | 4 | 6 |
| α-helix | 325-341 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transducin | A, B, C | protein | 324 | Bos taurus | P04695 (AlphaFold model) |
>1TND_1 TRANSDUCIN (chains A, B, C) ARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTT LNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLND SAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKK WIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNK KDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQ NVKFVFDAVTDIIIKENLKDCGLF
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 3 |
| CAC | Cacodylate ion | C2 H6 As O2 | 6 |
| GSP | 5'-guanosine-diphosphate-monothiophosphate | C10 H16 N5 O13 P3 S | 3 |
The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S. Noel, J.P., Hamm, H.E., Sigler, P.B. Nature (1993) 366:654-663. DOI 10.1038/366654a0 · PubMed
Other PDB entries of the same protein (UniProt P04695 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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