MolNFT v1 · #120093 · protein
Eukaryotic RAD50 functions as a rod-shaped dimer
5GOX · DNA repair protein RAD50: “Eukaryotic RAD50 functions as a rod-shaped dimer”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.56). MolNFT v1 #120093 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5GOX
- Type
- protein
- Length
- 362 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein RAD50
- EC
- 3.6.-.-
- UniProt
- Q92878
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 85% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA repair protein RAD50 (EC 3.6.-.-) | protein | 181 | 85% helix, 1% strand | Q92878 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.56 | 0.79 | 27 | empty |
| 2 | 232 | 0.46 | 0.73 | 34 | empty |
| 3 | 70 | 0.35 | 0.76 | 15 | empty |
| 4 | 59 | 0.33 | 0.77 | 10 | empty |
| 5 | 58 | 0.27 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1253 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 Q92878
- Elsewhere: RCSB PDB 5GOX · PDBe 5GOX · UniProt Q92878
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.