Research workbench
Crystal structure of the human RAD52 protein
Analyse Crystal structure of the human RAD52 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KN0
- Type
- protein
- Length
- 2,024 residues
- Chains
- 11
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAD52
- UniProt
- P43351
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K | RAD52 | protein | 184 | 36% helix, 28% strand | P43351 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 609 | 0.76 | 0.82 | 75 | empty |
| 2 | 565 | 0.75 | 0.82 | 78 | empty |
| 3 | 323 | 0.73 | 0.85 | 64 | empty |
| 4 | 434 | 0.71 | 0.82 | 60 | empty |
| 5 | 156 | 0.63 | 0.85 | 32 | empty |
Interfaces
22 interfaces between chains.
- F–G · 2633 Ų buried · 47 hydrogen bonds · protein-protein
- E–F · 2622 Ų buried · 43 hydrogen bonds · protein-protein
- D–E · 2617 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 2617 Ų buried · 36 hydrogen bonds · protein-protein
- C–D · 2614 Ų buried · 40 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 P43351
- Elsewhere: RCSB PDB 1KN0 · PDBe 1KN0 · UniProt P43351
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