Research workbench
Molecular structure of promoter-bound yeast tfiid
Analyse Molecular structure of promoter-bound yeast tfiid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HQA
- Type
- protein
- Length
- 2,551 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TAF2; Subunit (90 kda) of tfiid and saga complexes; Subunit (60 kda) of tfiid and saga…
- UniProt
- C4R4L4, C4QW33, C4QZS5, C4R150, C4R420
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 11 distinct chains · 50% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TAF2 | protein | 887 | 42% helix, 8% strand | — |
| B | Subunit (90 kda) of tfiid and saga complexes | protein | 522 | 20% helix, 18% strand | C4R4L4 |
| C | Subunit (90 kda) of tfiid and saga complexes | protein | 136 | 65% helix, 0% strand | C4R4L4 |
| D | Subunit (60 kda) of tfiid and saga complexes | protein | 254 | 68% helix, 0% strand | C4QW33 |
| E | Subunit (60 kda) of tfiid and saga complexes | protein | 320 | 74% helix, 0% strand | C4QW33 |
| F | Subunit (17 kda) of tfiid and saga complexes, involved in RNA polymerase II transcription initiation | protein | 103 | 57% helix, 0% strand | C4QZS5 |
| G | TAF8 | protein | 75 | 85% helix, 0% strand | — |
| I | Histone-fold | protein | 64 | 70% helix, 0% strand | — |
| H | Histone-fold | protein | 68 | 72% helix, 0% strand | — |
| K | Subunit (61/68 kda) of tfiid and saga complexes | protein | 71 | 73% helix, 0% strand | C4R150 |
| J | Tfiid subunit (48 kda) | protein | 51 | 75% helix, 0% strand | C4R420 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.77 | 0.81 | 108 | empty |
| 2 | 808 | 0.76 | 0.80 | 116 | empty |
| 3 | 1120 | 0.76 | 0.78 | 117 | empty |
| 4 | 763 | 0.76 | 0.81 | 102 | empty |
| 5 | 1087 | 0.74 | 0.77 | 101 | empty |
Interfaces
12 interfaces between chains.
- E–F · 796 Ų buried · 2 hydrogen bonds · protein-protein
- K–J · 423 Ų buried · 1 hydrogen bond · protein-protein
- B–H · 231 Ų buried · 1 hydrogen bond · protein-protein
- I–H · 218 Ų buried · 0 hydrogen bonds · protein-protein
- A–G · 216 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6HQA · Molecular structure of promoter-bound yeast TFIID · the same entry in another collection · chain A against A, TM-score 1.00
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 C4R4L4
- Every structure of UniProt C4QW33
- Every structure of UniProt C4QZS5
- Every structure of UniProt C4R150
- Every structure of UniProt C4R420
- Elsewhere: RCSB PDB 6HQA · PDBe 6HQA · UniProt C4R4L4 · UniProt C4QW33 · UniProt C4QZS5 · UniProt C4R150 · UniProt C4R420
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