MolNFT v1 · #86970 · protein
Crystal structure of ribonucleotide reductase apo-nrdf from bacillus cereus (space group C2)
4BMQ · Ribonucleoside-diphosphate reductase subunit beta: “Crystal structure of ribonucleotide reductase apo-nrdf from bacillus cereus (space group C2)”. X-ray diffraction, 1 ligand (FE2), 6 pockets (best druggability 0.49). MolNFT v1…
- PDB
- 4BMQ
- Type
- protein
- Length
- 587 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase subunit beta
- EC
- 1.17.4.1
- UniProt
- Q81G55
- Ligands
- FE2
- Pockets
- 6 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase subunit beta (EC 1.17.4.1) | protein | 300 | 75% helix, 0% strand | Q81G55 |
| B | Ribonucleoside-diphosphate reductase subunit beta (EC 1.17.4.1) | protein | 287 | 78% helix, 0% strand | Q81G55 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.49 | 0.76 | 28 | empty |
| 2 | 63 | 0.41 | 0.80 | 13 | empty |
| 3 | 96 | 0.40 | 0.76 | 17 | empty |
| 4 | 89 | 0.37 | 0.75 | 19 | empty |
| 5 | 55 | 0.33 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2316 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 4BMQ · Crystal Structure of Ribonucleotide Reductase apo-NrdF from Bacillus cereus (space group… · 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 Q81G55
- Elsewhere: RCSB PDB 4BMQ · PDBe 4BMQ · UniProt Q81G55
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