MolNFT v1 · #119197 · protein
Humanised monomeric rada in complex with oligomerisation peptide
5FOS · DNA repair and recombination protein rada: “Humanised monomeric rada in complex with oligomerisation peptide”. X-ray diffraction, 2 ligands (NH2, PO4), 3 pockets (best druggability 0.54). MolNFT v1 #119197 on GenesisL1: 3D…
- PDB
- 5FOS
- Type
- protein
- Length
- 240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair and recombination protein rada
- EC
- 3.6.4.-
- UniProt
- O74036
- Ligands
- NH2, PO4
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair and recombination protein rada (EC 3.6.4.-) | protein | 225 | 38% helix, 26% strand | O74036 |
| C | DNA repair and recombination protein rada (EC 3.6.4.-) | protein | 15 | 53% helix, 13% strand | O74036 |
Ligands and binding sites
- NH2 · Amino group · ion · chains C
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.54 | 0.79 | 23 | empty |
| 2 | 83 | 0.37 | 0.77 | 16 | PO4 |
| 3 | 54 | 0.35 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–C · 638 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5FOS · Humanised monomeric rada in complex with oligomerisation peptide · 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 0.97
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 5FOS · PDBe 5FOS · UniProt O74036
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