MolNFT v1 · #182304 · protein
Crystal structure of the class ie ribonucleotide reductase beta subunit from aerococcus urinae (in alternate conformation)
7MMW · Ribonucleoside-diphosphate reductase: “Crystal structure of the class ie ribonucleotide reductase beta subunit from aerococcus urinae (in alternate…”. X-ray diffraction, 1 ligand (CA), 5 pockets (best druggability 0.53). MolNFT v1…
- PDB
- 7MMW
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase
- EC
- 1.17.4.1
- UniProt
- F2I8X9
- Ligands
- CA
- Pockets
- 5 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase (EC 1.17.4.1) | protein | 319 | 75% helix, 1% strand | F2I8X9 |
| B | Ribonucleoside-diphosphate reductase (EC 1.17.4.1) | protein | 309 | 76% helix, 1% strand | F2I8X9 |
Ligands and binding sites
- CA · Calcium ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.53 | 0.80 | 36 | empty |
| 2 | 106 | 0.40 | 0.76 | 15 | empty |
| 3 | 63 | 0.40 | 0.80 | 21 | empty |
| 4 | 51 | 0.33 | 0.78 | 13 | empty |
| 5 | 61 | 0.32 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2773 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 7MMW · Crystal Structure of the Class Ie Ribonucleotide Reductase Beta Subunit from Aerococcus… · 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 F2I8X9
- Elsewhere: RCSB PDB 7MMW · PDBe 7MMW · UniProt F2I8X9
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