MolNFT v1 · #75084 · protein
Pwwp domain of human bromodomain and phd finger-containing protein 3
3PFS: “Pwwp domain of human bromodomain and phd finger-containing protein 3”. X-ray diffraction, 2 ligands (ZN, SO4), 5 pockets (best druggability 0.74). MolNFT v1 #75084 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3PFS
- Type
- protein
- Length
- 264 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain and phd finger-containing protein 3
- UniProt
- Q9ULD4
- Ligands
- ZN, SO4
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain and phd finger-containing protein 3 | protein | 134 | 33% helix, 24% strand | Q9ULD4 |
| B | Bromodomain and phd finger-containing protein 3 | protein | 130 | 33% helix, 20% strand | Q9ULD4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 822 | 0.74 | 0.78 | 58 | empty |
| 2 | 154 | 0.56 | 0.81 | 28 | empty |
| 3 | 98 | 0.37 | 0.75 | 21 | empty |
| 4 | 61 | 0.33 | 0.76 | 17 | ZN |
| 5 | 57 | 0.32 | 0.76 | 19 | ZN |
Interfaces
1 interface between chains.
- A–B · 692 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3PFS · PWWP Domain of Human Bromodomain and PHD finger-containing protein 3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULD4 · AlphaFold monomer V2.0 prediction for bromodomain and phd finger- containing protein 3… · a predicted model of the same protein · chain B against A, TM-score 0.90
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 Q9ULD4
- Elsewhere: RCSB PDB 3PFS · PDBe 3PFS · UniProt Q9ULD4
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