MolNFT v1 · #120485 · protein
Complex structure of TRIM24 phd-bromodomain and inhibitor 6
5H1V · Transcription intermediary factor 1-alpha: “Complex structure of TRIM24 phd-bromodomain and inhibitor 6”. X-ray diffraction, 2 ligands (7FU, ZN), 2 pockets (best druggability 0.45). MolNFT v1 #120485 on GenesisL1: 3D structure…
- PDB
- 5H1V
- Type
- protein
- Length
- 339 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription intermediary factor 1-alpha
- EC
- 6.3.2.-
- UniProt
- O15164
- Ligands
- 7FU, ZN
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription intermediary factor 1-alpha (EC 6.3.2.-) | protein | 169 | 45% helix, 2% strand | O15164 |
| B | Transcription intermediary factor 1-alpha (EC 6.3.2.-) | protein | 170 | 45% helix, 2% strand | O15164 |
Ligands and binding sites
- 7FU · 2-Hydrazino-1,3-benzothiazole-6-carbohydrazide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- DMS · Dimethyl sulfoxide · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.45 | 0.82 | 16 | 7FU |
| 2 | 66 | 0.44 | 0.82 | 19 | 7FU |
Compared structures
- 5H1V · Complex structure of TRIM24 PHD-bromodomain and inhibitor 6 · the same entry in another collection · chain A against A, TM-score 1.00
- O15164 · AlphaFold monomer V2.0 prediction for transcription intermediary factor 1-alpha (O15164) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O15164
- Elsewhere: RCSB PDB 5H1V · PDBe 5H1V · UniProt O15164
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