Research workbench
The structure of OSALKBH1
Analyse The structure of OSALKBH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XOI
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxidoreductase, 2OG-fe oxygenase family protein, putative, expressed
- UniProt
- Q10BI6
- Ligands
- MN
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase, 2OG-fe oxygenase family protein, putative, expressed | protein | 227 | 24% helix, 35% strand | Q10BI6 |
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 | 150 | 0.79 | 0.95 | 33 | SIN |
| 2 | 65 | 0.44 | 0.81 | 12 | empty |
Compared structures
- 5XOI · The structure of OsALKBH1 · 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 Q10BI6
- Elsewhere: RCSB PDB 5XOI · PDBe 5XOI · UniProt Q10BI6
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