Research workbench
Crystal structure of a yeast TBP/TATA-box complex
Analyse Crystal structure of a yeast TBP/TATA-box complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YTB
- Type
- protein + DNA
- Length
- 418 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (29MER); Protein (tata binding protein (tbp))
- UniProt
- P13393
- Pockets
- 6 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | DNA (29MER) | dna | 29 | — | — |
| A, B | Protein (tata binding protein (tbp)) | protein | 180 | 27% helix, 34% strand | P13393 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.53 | 0.74 | 46 | empty |
| 2 | 53 | 0.34 | 0.79 | 13 | empty |
| 3 | 103 | 0.32 | 0.72 | 13 | empty |
| 4 | 62 | 0.32 | 0.76 | 14 | empty |
| 5 | 87 | 0.31 | 0.73 | 12 | empty |
Interfaces
3 interfaces between chains.
- C–A · 1508 Ų buried · 13 hydrogen bonds · protein-nucleic
- D–B · 1462 Ų buried · 16 hydrogen bonds · protein-nucleic
- A–B · 114 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P13393
- Elsewhere: RCSB PDB 1YTB · PDBe 1YTB · UniProt P13393
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