Research workbench
Crystal structure of the BARD1 brct repeat
Analyse Crystal structure of the BARD1 brct repeat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R1Z
- Type
- protein
- Length
- 410 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BRCA1-associated ring domain protein 1
- UniProt
- Q99728
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BRCA1-associated ring domain protein 1 | protein | 202 | 35% helix, 16% strand | Q99728 |
| B | BRCA1-associated ring domain protein 1 | protein | 208 | 35% helix, 16% strand | Q99728 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
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 | 298 | 0.66 | 0.81 | 39 | empty |
| 2 | 288 | 0.65 | 0.81 | 38 | empty |
| 3 | 52 | 0.33 | 0.77 | 8 | empty |
| 4 | 51 | 0.31 | 0.77 | 17 | empty |
| 5 | 57 | 0.26 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 683 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 Q99728
- Elsewhere: RCSB PDB 2R1Z · PDBe 2R1Z · UniProt Q99728
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.