MolNFT v1 · #20555 · protein
Structure and function of the escherichia COLI ribonucleotide reductase protein R2
1RIB · Ribonucleotide reductase R1 protein: “Structure and function of the escherichia COLI ribonucleotide reductase protein R2”. X-ray diffraction, 1 ligand (FEO), 3 pockets (best druggability 0.74). MolNFT v1 #20555 on GenesisL1: 3D…
- PDB
- 1RIB
- Type
- protein
- Length
- 680 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleotide reductase R1 protein
- EC
- 1.17.4.1
- UniProt
- P69924
- Ligands
- FEO
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonucleotide reductase R1 protein (EC 1.17.4.1) | protein | 340 | 70% helix, 4% strand | P69924 |
Ligands and binding sites
- FEO · Mu-oxo-diiron · ligand · 2 copies · chains A, B
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 | 128 | 0.74 | 0.93 | 27 | empty |
| 2 | 69 | 0.52 | 0.86 | 18 | empty |
| 3 | 50 | 0.26 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 3081 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 1RIB · Structure and function of the escherichia COLI ribonucleotide reductase protein R2 · 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 P69924
- Elsewhere: RCSB PDB 1RIB · PDBe 1RIB · UniProt P69924
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