Crystal structure of yeast tata-binding protein and model for interaction with DNA. Determined by X-ray diffraction at 2.6 Å resolution. Released 31 Jan 1994.
Explore 1TBP in 3D Show helices and sheets RCSB PDB PDBe
1TBP contains 8 α-helices and 25 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 |
|---|---|---|---|
| β-strand | 66-75 | 10 | 1 |
| α-helix | 82-89 | 8 | |
| β-strand | 93 | 1 | 1 |
| β-strand | 102-106 | 5 | 1 |
| β-strand | 111-115 | 5 | 1 |
| β-strand | 120-126 | 7 | 1 |
| α-helix | 129-142 | 14 | |
| β-strand | 156-165 | 10 | 1 |
| β-strand | 170 | 1 | 2 |
| α-helix | 172-178 | 7 | |
| β-strand | 183-184 | 2 | 1 |
| β-strand | 193-197 | 5 | 1 |
| β-strand | 202-206 | 5 | 1 |
| β-strand | 211-217 | 7 | 1 |
| α-helix | 221-236 | 16 | |
| β-strand | 238 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 66-75 | 10 | 3 |
| α-helix | 82-86 | 5 | |
| β-strand | 95 | 1 | 4 |
| β-strand | 99 | 1 | 4 |
| β-strand | 102-105 | 4 | 3 |
| β-strand | 112-115 | 4 | 3 |
| β-strand | 120-126 | 7 | 3 |
| α-helix | 129-146 | 18 | |
| β-strand | 153-165 | 13 | 3 |
| β-strand | 170 | 1 | 5 |
| α-helix | 172-178 | 7 | |
| β-strand | 183-184 | 2 | 3 |
| β-strand | 193-198 | 6 | 3 |
| β-strand | 201-206 | 6 | 3 |
| β-strand | 211-215 | 5 | 3 |
| α-helix | 220-234 | 15 | |
| β-strand | 238 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tata-binding protein | A, B | protein | 180 | Saccharomyces cerevisiae | P13393 (AlphaFold model) |
>1TBP_1 TATA-BINDING PROTEIN (chains A, B) MGIVPTLQNIVATVTLGCRLDLKTVALHARNAEYNPKRFAAVIMRIREPKTTALIFASGK MVVTGAKSEDDSKLASRKYARIIQKIGFAAKFTDFKIQNIVGSCDVKFPIRLEGLAFSHG TFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKQREEIYQAFEAIYPVLSEFRKM
Crystal structure of yeast TATA-binding protein and model for interaction with DNA. Chasman, D.I., Flaherty, K.M., Sharp, P.A. et al. Proc Natl Acad Sci U S A (1993) 90:8174-8178. DOI 10.1073/pnas.90.17.8174 · PubMed
Other PDB entries of the same protein (UniProt P13393 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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