Crystal structure of a ternary complex of the transcriptional repressor Gal80p (Gal80S0 [G301R]) and the acidic activation domain of Gal4p (aa 854-874) from Saccharomyces cerevisiae with NAD. Determined by X-ray diffraction at 2.7 Å resolution. Released 4 Mar 2008.
Explore 3BTS in 3D Show helices and sheets RCSB PDB PDBe
3BTS contains 36 α-helices and 38 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 | 17 | 1 | |
| β-strand | 18-23 | 6 | 1 |
| α-helix | 31-34 | 4 | |
| α-helix | 36-42 | 7 | |
| β-strand | 47-53 | 7 | 1 |
| α-helix | 57-66 | 10 | |
| β-strand | 73-75 | 3 | 1 |
| α-helix | 78-83 | 6 | |
| β-strand | 89-92 | 4 | 1 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-109 | 11 | |
| α-helix | 110-112 | 3 | |
| β-strand | 118-121 | 4 | 1 |
| α-helix | 122 | 1 | |
| α-helix | 129-142 | 14 | |
| β-strand | 145-148 | 4 | 1 |
| α-helix | 151-154 | 4 | |
| α-helix | 156-166 | 11 | |
| β-strand | 173-181 | 9 | 2 |
| β-strand | 188-190 | 3 | 3 |
| α-helix | 196-198 | 3 | |
| α-helix | 206-211 | 6 | |
| α-helix | 212-221 | 10 | |
| β-strand | 226-234 | 9 | 2 |
| β-strand | 239-243 | 5 | 3 |
| β-strand | 249-255 | 7 | 3 |
| β-strand | 261-268 | 8 | 2 |
| α-helix | 270-272 | 3 | |
| β-strand | 274-280 | 7 | 2 |
| β-strand | 292-298 | 7 | 2 |
| β-strand | 302-307 | 6 | 2 |
| β-strand | 314-321 | 8 | 2 |
| β-strand | 349-353 | 5 | 2 |
| α-helix | 360-378 | 19 | |
| α-helix | 402-421 | 20 | |
| β-strand | 423 | 1 | 4 |
| β-strand | 425-426 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-17 | 2 | |
| β-strand | 18-23 | 6 | 5 |
| α-helix | 31-34 | 4 | |
| α-helix | 36-42 | 7 | |
| β-strand | 47-53 | 7 | 5 |
| α-helix | 57-66 | 10 | |
| β-strand | 73-75 | 3 | 5 |
| α-helix | 78-83 | 6 | |
| β-strand | 89-92 | 4 | 5 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-109 | 11 | |
| α-helix | 110-112 | 3 | |
| β-strand | 118-121 | 4 | 5 |
| α-helix | 122 | 1 | |
| α-helix | 129-142 | 14 | |
| β-strand | 145-148 | 4 | 5 |
| α-helix | 151-154 | 4 | |
| α-helix | 156-166 | 11 | |
| β-strand | 173-181 | 9 | 6 |
| β-strand | 188-190 | 3 | 7 |
| α-helix | 196-198 | 3 | |
| α-helix | 206-211 | 6 | |
| α-helix | 212-221 | 10 | |
| β-strand | 226-234 | 9 | 6 |
| β-strand | 239-243 | 5 | 7 |
| β-strand | 249-255 | 7 | 7 |
| β-strand | 261-268 | 8 | 6 |
| α-helix | 270-272 | 3 | |
| β-strand | 274-280 | 7 | 6 |
| β-strand | 292-298 | 7 | 6 |
| β-strand | 301-307 | 7 | 6 |
| β-strand | 316-321 | 6 | 6 |
| β-strand | 349-353 | 5 | 6 |
| α-helix | 360-376 | 17 | |
| α-helix | 402-421 | 20 | |
| β-strand | 423 | 1 | 4 |
| β-strand | 425-426 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Galactose/lactose metabolism regulatory protein GAL80 | A, B | protein | 438 | Saccharomyces cerevisiae | P04387 (AlphaFold model) |
| Regulatory protein GAL4 | E, F | protein | 21 | P04386 (AlphaFold model) |
>3BTS_1 Galactose/lactose metabolism regulatory protein GAL80 (chains A, B) GSHMDYNKRSSVSTVPNAAPIRVGFVGLNAAKGWAIKTHYPAILQLSSQFQITALYSPKI ETSIATIQRLKLSNATAFPTLESFASSSTIDMIVIAIQVASHYEVVMPLLEFSKNNPNLK YLFVEWALACSLDQAESIYKAAAERGVQTIISLQGRKSPYILRAKELISQGYIGDINSIE IAGNGGWYGYERPVKSPKYIYEIGNGVDLVTTTFGHTIDILQYMTSSYFSRINAMVFNNI PEQELIDERGNRLGQRVPKTVPDHLLFQGTLLNGNVPVSCSFKGGKPTKKFTKNLVIDIH GTKRDLKLEGDAGFAEISNLVLYYSGTRANDFPLANGQQAPLDPGYDAGKEIMEVYHLRN YNAIVGNIHRLYQSISDFHFNTKKIPELPSQFVMQGFDFEGFPTLMDALILHRLIESVYK SNMMGSTLNVSNISHYSL
>3BTS_2 Regulatory protein GAL4 (chains E, F) GMFNTTTMDDVYNYLFDDEDT
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAD | Nicotinamide-adenine-dinucleotide | C21 H27 N7 O14 P2 | 2 |
NADP regulates the yeast GAL induction system. Kumar, P.R., Yu, Y., Sternglanz, R. et al. Science (2008) 319:1090-1092. DOI 10.1126/science.1151903 · PubMed
Other PDB entries of the same protein (UniProt P04387 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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