Research workbench
Crystal structure of TAF1-TAF7, a tfiid subcomplex
Analyse Crystal structure of TAF1-TAF7, a tfiid subcomplex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OY2
- Type
- protein
- Length
- 2,077 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription initiation factor tfiid subunit 1; Transcription initiation factor tfiid…
- EC
- 2.3.1.48
- UniProt
- P46677, Q05021
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 5 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 1 (EC 2.3.1.48) | protein | 470 | 32% helix, 20% strand | P46677 |
| C | Transcription initiation factor tfiid subunit 1 (EC 2.3.1.48) | protein | 460 | 33% helix, 19% strand | P46677 |
| E | Transcription initiation factor tfiid subunit 1 (EC 2.3.1.48) | protein | 468 | 33% helix, 20% strand | P46677 |
| B | Transcription initiation factor tfiid subunit 7 | protein | 229 | 28% helix, 29% strand | Q05021 |
| D, F | Transcription initiation factor tfiid subunit 7 | protein | 225 | 30% helix, 28% strand | Q05021 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 339 | 0.86 | 0.96 | 51 | empty |
| 2 | 725 | 0.86 | 0.89 | 86 | empty |
| 3 | 362 | 0.86 | 0.95 | 57 | empty |
| 4 | 919 | 0.82 | 0.84 | 88 | empty |
| 5 | 400 | 0.77 | 0.86 | 47 | empty |
Interfaces
10 interfaces between chains.
- E–F · 7063 Ų buried · 130 hydrogen bonds · protein-protein
- A–B · 7007 Ų buried · 126 hydrogen bonds · protein-protein
- C–D · 6741 Ų buried · 111 hydrogen bonds · protein-protein
- A–E · 926 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 729 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 48 modified (engineered).
Compared structures
- 4OY2 · Crystal structure of TAF1-TAF7, a TFIID subcomplex · the same entry in another collection · chain F against F, TM-score 1.00
- Q05021 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 7… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P46677 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 1… · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P46677
- Every structure of UniProt Q05021
- Elsewhere: RCSB PDB 4OY2 · PDBe 4OY2 · UniProt P46677 · UniProt Q05021
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