MolNFT v1 · #86308 · protein
Rada C-terminal ATPase domain from pyrococcus furiosus bound to GTP
4B2P · DNA repair and recombination protein rada: “Rada C-terminal ATPase domain from pyrococcus furiosus bound to GTP”. X-ray diffraction, 2 ligands (GTP, MG), 2 pockets (best druggability 0.45). MolNFT v1 #86308 on GenesisL1: 3D…
- PDB
- 4B2P
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair and recombination protein rada
- UniProt
- O74036
- Ligands
- GTP, MG
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair and recombination protein rada | protein | 216 | 40% helix, 26% strand | O74036 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.45 | 0.78 | 19 | empty |
| 2 | 51 | 0.27 | 0.75 | 14 | GTP, MG |
Compared structures
- 4B2P · RadA C-terminal ATPase domain from Pyrococcus furiosus bound to GTP · the same entry in another collection · chain A against A, TM-score 1.00
- O74036 · AlphaFold monomer V2.0 prediction for DNA repair and recombination protein rada (O74036) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O74036
- Elsewhere: RCSB PDB 4B2P · PDBe 4B2P · UniProt O74036
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