Research workbench
Crystal structure of the BRCA1 associated ring domain (BARD1) tandem brct domains
Analyse Crystal structure of the BRCA1 associated ring domain (BARD1) tandem brct… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FA2
- Type
- protein
- Length
- 408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BRCA1-associated ring domain protein 1
- UniProt
- Q99728
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BRCA1-associated ring domain protein 1 | protein | 203 | 33% helix, 16% strand | Q99728 |
| B | BRCA1-associated ring domain protein 1 | protein | 205 | 35% helix, 16% strand | Q99728 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 713 | 0.73 | 0.79 | 61 | empty |
| 2 | 68 | 0.30 | 0.73 | 14 | PO4 |
| 3 | 51 | 0.26 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 602 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3FA2 · Crystal Structure of the BRCA1 Associated Ring Domain (BARD1) Tandem BRCT Domains · the same entry in another collection · chain A against A, TM-score 1.00
- Q99728 · AlphaFold monomer V2.0 prediction for BRCA1-associated ring domain protein 1 (Q99728) · a predicted model of the same protein · chain A 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 Q99728
- Elsewhere: RCSB PDB 3FA2 · PDBe 3FA2 · UniProt Q99728
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