MolNFT v1 · #129510 · protein
R2-like ligand-binding oxidase with aerobically reconstituted metal cofactor after photoconversion
5OMJ · Ribonucleotide reductase small subunit: “R2-like ligand-binding oxidase with aerobically reconstituted metal cofactor after photoconversion”. X-ray diffraction, 2 ligands (PLM, FE), 2 pockets (best druggability 0.84). MolNFT v1…
- PDB
- 5OMJ
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleotide reductase small subunit
- EC
- 1.17.4.1
- UniProt
- Q5KW80
- Ligands
- PLM, FE
- Pockets
- 2 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleotide reductase small subunit (EC 1.17.4.1) | protein | 285 | 79% helix, 0% strand | Q5KW80 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.84 | 0.96 | 43 | FE, PLM |
| 2 | 79 | 0.34 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 5OMJ · R2-like ligand-binding oxidase with aerobically reconstituted metal cofactor after… · 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 Q5KW80
- Elsewhere: RCSB PDB 5OMJ · PDBe 5OMJ · UniProt Q5KW80
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