MolNFT v2 · #12444 · protein
R2F from Corynebacterium Ammoniagenes in its reduced, Fe containing, form
1KGO · Ribonucleotide reductase protein R2F: “R2F from Corynebacterium Ammoniagenes in its reduced, Fe containing, form”. X-ray diffraction at 2.25, 1 ligand (FE2), 7 pockets (best druggability 0.57). MolNFT v2 #12444 on GenesisL1: 3D…
- PDB
- 1KGO
- Type
- protein
- Length
- 1,184 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.25
- Source
- Corynebacterium ammoniagenes
- Molecule
- Ribonucleotide reductase protein R2F
- UniProt
- O69274
- Ligands
- FE2
- Pockets
- 7 · best druggability 0.57
Structure
x-ray diffraction · resolution 2.25 · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ribonucleotide reductase protein R2F | protein | 296 | 78% helix, 0% strand | O69274 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.57 | 0.79 | 35 | empty |
| 2 | 320 | 0.54 | 0.74 | 41 | empty |
| 3 | 315 | 0.53 | 0.74 | 44 | empty |
| 4 | 62 | 0.33 | 0.76 | 15 | empty |
| 5 | 62 | 0.32 | 0.76 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2773 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2761 Ų buried · 22 hydrogen bonds · protein-protein
- A–D · 254 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1KGO · R2F from corynebacterium ammoniagenes in its reduced, fe containing, form · the same entry in another collection · chain A 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 O69274
- Elsewhere: RCSB PDB 1KGO · PDBe 1KGO · UniProt O69274
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