MolNFT v1 · #115388 · protein
Ribonucleotide reductase beta subunit
5CI4 · Ribonucleoside-diphosphate reductase 1, beta subunit…: “Ribonucleotide reductase beta subunit”. X-ray diffraction, 2 ligands (FEO, SO4), 1 pocket (best druggability 0.28). MolNFT v1 #115388 on GenesisL1: 3D structure, binding sites…
- PDB
- 5CI4
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein
- EC
- 1.17.4.1
- UniProt
- A0A0E1LZC3
- Ligands
- FEO, SO4
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein (EC 1.17.4.1) | protein | 349 | 68% helix, 4% strand | A0A0E1LZC3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.28 | 0.74 | 14 | empty |
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 A0A0E1LZC3
- Elsewhere: RCSB PDB 5CI4 · PDBe 5CI4 · UniProt A0A0E1LZC3
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