Research workbench
Plasmodium vivax ribonucleotide reductase subunit R2 (PV086155)
Analyse Plasmodium vivax ribonucleotide reductase subunit R2 (PV086155) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O1Z
- Type
- protein
- Length
- 567 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleotide reductase subunit R2
- UniProt
- A5K1H0
- Ligands
- FE, UNX
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleotide reductase subunit R2 | protein | 288 | 68% helix, 1% strand | A5K1H0 |
| B | Ribonucleotide reductase subunit R2 | protein | 279 | 68% helix, 0% strand | A5K1H0 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
- UNX · Unknown atom or ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 721 | 0.73 | 0.79 | 43 | empty |
| 2 | 445 | 0.62 | 0.76 | 39 | empty |
| 3 | 184 | 0.53 | 0.78 | 26 | empty |
| 4 | 146 | 0.52 | 0.80 | 25 | empty |
| 5 | 52 | 0.38 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1265 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2O1Z · Plasmodium vivax Ribonucleotide Reductase Subunit R2 (Pv086155) · 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 A5K1H0
- Elsewhere: RCSB PDB 2O1Z · PDBe 2O1Z · UniProt A5K1H0
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