Research workbench
Crystal structure of a PALB2 / BRCA2 complex
Analyse Crystal structure of a PALB2 / BRCA2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EU7
- Type
- protein
- Length
- 327 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Partner and localizer of BRCA2; 19MERIC peptide from breast cancer type 2 susceptibility…
- UniProt
- Q86YC2, P51587
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Partner and localizer of BRCA2 | protein | 313 | 0% helix, 58% strand | Q86YC2 |
| X | 19MERIC peptide from breast cancer type 2 susceptibility protein | protein | 14 | 36% helix, 0% strand | P51587 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 852 | 0.75 | 0.79 | 63 | empty |
| 2 | 50 | 0.37 | 0.80 | 18 | GOL |
Interfaces
1 interface between chains.
- A–X · 600 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (oxidation).
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 Q86YC2
- Every structure of UniProt P51587
- Elsewhere: RCSB PDB 3EU7 · PDBe 3EU7 · UniProt Q86YC2 · UniProt P51587
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