Research workbench
Crystal structure of C239S mutant of a novel disulfide oxidoreductase from deinococcus radiodurans
Analyse Crystal structure of C239S mutant of a novel disulfide oxidoreductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CP1
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frne protein
- UniProt
- Q9RWK7
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frne protein | protein | 245 | 49% helix, 11% strand | Q9RWK7 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
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 | 243 | 0.66 | 0.83 | 28 | GOL |
| 2 | 82 | 0.48 | 0.82 | 17 | EDO |
Compared structures
- 5CP1 · Crystal structure of C239S mutant of a novel disulfide oxidoreductase from Deinococcus… · 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 Q9RWK7
- Elsewhere: RCSB PDB 5CP1 · PDBe 5CP1 · UniProt Q9RWK7
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