MolNFT v1 · #20038 · protein
Ribonucleotide reductase R2F protein from salmonella typhimurium
1R2F · Protein (ribonucleotide reductase R2): “Ribonucleotide reductase R2F protein from salmonella typhimurium”. X-ray diffraction, 1 ligand (FE), 2 pockets (best druggability 0.39). MolNFT v1 #20038 on GenesisL1: 3D structure, binding…
- PDB
- 1R2F
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (ribonucleotide reductase R2)
- EC
- 1.17.4.1
- UniProt
- P17424
- Ligands
- FE
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (ribonucleotide reductase R2) (EC 1.17.4.1) | protein | 283 | 78% helix, 0% strand | P17424 |
| B | Protein (ribonucleotide reductase R2) (EC 1.17.4.1) | protein | 281 | 79% helix, 0% strand | P17424 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B
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 | 65 | 0.39 | 0.79 | 17 | empty |
| 2 | 57 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1807 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1R2F · Ribonucleotide reductase R2F protein from salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
- P17424 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 2 subunit beta… · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P17424
- Elsewhere: RCSB PDB 1R2F · PDBe 1R2F · UniProt P17424
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