Research workbench
Alpha-ketoglutarate-dependent dioxygenase alkb in complex with fe and akg after oxygen exposure using ft-ssx methods
Analyse Alpha-ketoglutarate-dependent dioxygenase alkb in complex with fe and akg after… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YPV
- Type
- protein
- Length
- 199 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-ketoglutarate-dependent dioxygenase alkb
- EC
- 1.14.11.33
- UniProt
- P05050
- Ligands
- AKG, FE
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent dioxygenase alkb (EC 1.14.11.33) | protein | 199 | 16% helix, 35% strand | P05050 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.68 | 0.86 | 39 | FE, AKG |
Compared structures
- 6YPV · Alpha-ketoglutarate-dependent dioxygenase AlkB in complex with Fe and AKG after oxygen… · the same entry in another collection · chain A against A, TM-score 1.00
- P05050 · AlphaFold monomer V2.0 prediction for alpha-ketoglutarate-dependent dioxygenase alkb… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P05050
- Elsewhere: RCSB PDB 6YPV · PDBe 6YPV · UniProt P05050
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