MolNFT v1 · #139396 · protein
The structure of OSALKBH1
5XEG · Oxidoreductase, 2OG-fe oxygenase family protein, putative…: “The structure of OSALKBH1”. X-ray diffraction, 2 ligands (AKG, MN), 2 pockets (best druggability 0.71). MolNFT v1 #139396 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5XEG
- Type
- protein
- Length
- 219 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
- AKG, MN
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase, 2OG-fe oxygenase family protein, putative, expressed | protein | 219 | 26% helix, 34% 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 | 99 | 0.71 | 0.94 | 32 | AKG, MN |
| 2 | 65 | 0.43 | 0.81 | 12 | empty |
Compared structures
- 5XEG · 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 5XEG · PDBe 5XEG · UniProt Q10BI6
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