Research workbench
Crystal structure of snoab, a cofactor-independent oxygenase from streptomyces nogalater, determined to 1.7 resolution
Analyse Crystal structure of snoab, a cofactor-independent oxygenase from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KG0
- Type
- protein
- Length
- 292 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Snoab
- UniProt
- O54259
- Ligands
- CL
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Snoab | protein | 97 | 39% helix, 34% strand | O54259 |
| B | Snoab | protein | 98 | 39% helix, 34% strand | O54259 |
| C | Snoab | protein | 97 | 39% helix, 34% strand | O54259 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.74 | 0.77 | 73 | EDO |
| 2 | 142 | 0.60 | 0.84 | 21 | EDO, CL |
| 3 | 97 | 0.50 | 0.81 | 21 | EDO |
Interfaces
2 interfaces between chains.
- A–C · 365 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 156 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3KG0 · Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater… · the same entry in another collection · chain A against A, TM-score 1.00
- O54259 · AlphaFold monomer V2.0 prediction for deoxynogalonate monooxygenase (O54259) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O54259
- Elsewhere: RCSB PDB 3KG0 · PDBe 3KG0 · UniProt O54259
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