MolNFT v1 · #178717 · protein
Crystal structure of the unliganded tandem bromodomain (BD1, BD2) of human TAF1
7JJH · Transcription initiation factor tfiid subunit 1: “Crystal structure of the unliganded tandem bromodomain (BD1, BD2) of human TAF1”. X-ray diffraction, 2 pockets (best druggability 0.51). MolNFT v1 #178717 on GenesisL1: 3D structure…
- PDB
- 7JJH
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription initiation factor tfiid subunit 1
- EC
- 2.3.1.48, 2.7.11.1
- UniProt
- P21675
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 1 (EC 2.3.1.48, 2.7.11.1) | protein | 253 | 67% helix, 0% strand | P21675 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.51 | 0.81 | 18 | EDO |
| 2 | 85 | 0.45 | 0.80 | 20 | empty |
Compared structures
- 7JJH · Crystal structure of the unliganded tandem bromodomain (BD1, BD2) of human TAF1 · the same entry in another collection · chain A against A, TM-score 1.00
- P21675 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 1… · a predicted model of the same protein · chain A against A, TM-score 0.58
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 P21675
- Elsewhere: RCSB PDB 7JJH · PDBe 7JJH · UniProt P21675
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