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Cystal structure of asparagine oxygenase in complex with FE(II), 2S, 3S-3-hydroxyasparagine and succinate
Analyse Cystal structure of asparagine oxygenase in complex with FE(II), 2S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OG7
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Asparagine oxygenase
- UniProt
- Q9Z4Z5
- Ligands
- AHB, FE2
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine oxygenase | protein | 319 | 30% helix, 22% strand | Q9Z4Z5 |
Ligands and binding sites
- AHB · Beta-hydroxyasparagine · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SIN · Succinic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.73 | 0.96 | 26 | SIN, AHB |
| 2 | 59 | 0.40 | 0.81 | 15 | empty |
| 3 | 63 | 0.37 | 0.79 | 16 | empty |
| 4 | 61 | 0.36 | 0.78 | 16 | empty |
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 Q9Z4Z5
- Elsewhere: RCSB PDB 2OG7 · PDBe 2OG7 · UniProt Q9Z4Z5
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