MolNFT v1 · #111701 · protein
Crystal structure of TAF1 BD2 bromodomain bound to a crotonyllysine peptide
4YYN · Transcription initiation factor tfiid subunit 1: “Crystal structure of TAF1 BD2 bromodomain bound to a crotonyllysine peptide”. X-ray diffraction, 1 pocket (best druggability 0.69). MolNFT v1 #111701 on GenesisL1: 3D structure…
- PDB
- 4YYN
- Type
- protein
- Length
- 269 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription initiation factor tfiid subunit 1; Histone H4
- UniProt
- P21675, P62805
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 1 | protein | 130 | 72% helix, 0% strand | P21675 |
| B | Transcription initiation factor tfiid subunit 1 | protein | 128 | 72% helix, 0% strand | P21675 |
| Z | Histone H4 | protein | 11 | 0% helix, 0% strand | P62805 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.69 | 0.93 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–Z · 583 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 487 Ų buried · 5 hydrogen bonds · protein-protein
- B–Z · 433 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 4YYN · Crystal structure of TAF1 BD2 Bromodomain bound to a crotonyllysine peptide · 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 B 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 P21675
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 4YYN · PDBe 4YYN · UniProt P21675 · UniProt P62805
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