MolNFT v1 · #74364 · protein
PHD2 with 2-oxoglutarate
3OUJ · Egl nine homolog 1: “PHD2 with 2-oxoglutarate”. X-ray diffraction, 3 ligands (AKG, FE2, SO4), 1 pocket (best druggability 0.68). MolNFT v1 #74364 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3OUJ
- Type
- protein
- Length
- 226 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Egl nine homolog 1
- EC
- 1.14.11.-
- UniProt
- Q9GZT9
- Ligands
- AKG, FE2, SO4
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Egl nine homolog 1 (EC 1.14.11.-) | protein | 226 | 29% helix, 31% strand | Q9GZT9 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
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 | 119 | 0.68 | 0.90 | 25 | FE2, AKG |
Compared structures
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 Q9GZT9
- Elsewhere: RCSB PDB 3OUJ · PDBe 3OUJ · UniProt Q9GZT9
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