Research workbench
High resolution structure of ribonucleotide reductase R2 from E. COLI in its oxidised (met) form
Analyse High resolution structure of ribonucleotide reductase R2 from E. COLI in its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MXR
- Type
- protein
- Length
- 678 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleotide reductase R2
- EC
- 1.17.4.1
- UniProt
- P69924
- Ligands
- HG, FE
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonucleotide reductase R2 (EC 1.17.4.1) | protein | 339 | 69% helix, 4% strand | P69924 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 11 copies · chains A, B
- FE · Fe (III) ion · metal · 4 copies · chains A, B
- GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.74 | 0.94 | 27 | empty |
| 2 | 73 | 0.59 | 0.88 | 20 | HG |
| 3 | 89 | 0.49 | 0.82 | 18 | HG |
Interfaces
1 interface between chains.
- A–B · 3142 Ų buried · 52 hydrogen bonds · protein-protein
Compared structures
- 1MXR · High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised… · the same entry in another collection · chain A against A, TM-score 1.00
- P69924 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 1 subunit beta… · 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 P69924
- Elsewhere: RCSB PDB 1MXR · PDBe 1MXR · UniProt P69924
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