Research workbench
Crystal structure of a RAD51-BRCA2 brc repeat complex
Analyse Crystal structure of a RAD51-BRCA2 brc repeat complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N0W
- Type
- protein
- Length
- 250 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein RAD51 homolog 1; Breast cancer type 2 susceptibility protein; Peptide…
- UniProt
- Q06609, P51587
- Ligands
- MG, CL
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein RAD51 homolog 1 | protein | 210 | 37% helix, 28% strand | Q06609 |
| B | Breast cancer type 2 susceptibility protein | protein | 33 | 27% helix, 9% strand | P51587 |
| L | Peptide linker | protein | 3 | 0% helix, 0% strand | — |
| C | Artificial gly-ser-mse-gly peptide | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 5 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.41 | 0.76 | 20 | empty |
| 2 | 66 | 0.34 | 0.76 | 15 | EDO |
Interfaces
2 interfaces between chains.
- A–B · 1078 Ų buried · 14 hydrogen bonds · protein-protein
- B–L · 59 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
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 Q06609
- Every structure of UniProt P51587
- Elsewhere: RCSB PDB 1N0W · PDBe 1N0W · UniProt Q06609 · UniProt P51587
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