Research workbench
Crystal structure of the bromo domain 1 in human bromodomain containing protein, testis specific (brdt)
Analyse Crystal structure of the bromo domain 1 in human bromodomain containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RFJ
- Type
- protein
- Length
- 315 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain testis-specific protein
- UniProt
- Q58F21
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain testis-specific protein | protein | 108 | 69% helix, 0% strand | Q58F21 |
| B | Bromodomain testis-specific protein | protein | 106 | 66% helix, 0% strand | Q58F21 |
| C | Bromodomain testis-specific protein | protein | 101 | 69% helix, 0% strand | Q58F21 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.49 | 0.79 | 31 | empty |
| 2 | 104 | 0.46 | 0.79 | 19 | empty |
| 3 | 58 | 0.30 | 0.75 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 764 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 689 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2RFJ · Crystal structure of the bromo domain 1 in human bromodomain containing protein, testis… · the same entry in another collection · chain A against A, TM-score 1.00
- Q58F21 · AlphaFold monomer V2.0 prediction for bromodomain testis-specific protein (Q58F21) · a predicted model of the same protein · chain C against A, TM-score 0.86
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 Q58F21
- Elsewhere: RCSB PDB 2RFJ · PDBe 2RFJ · UniProt Q58F21
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