Research workbench
Crystal structure of mouse myo-inositol oxygenase (re-refined)
Analyse Crystal structure of mouse myo-inositol oxygenase (re-refined) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BXD
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol oxygenase
- EC
- 1.13.99.1
- UniProt
- Q9QXN5
- Ligands
- INS, FE, OH
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol oxygenase (EC 1.13.99.1) | protein | 258 | 53% helix, 2% strand | Q9QXN5 |
Ligands and binding sites
- INS · 1,2,3,4,5,6-hexahydroxy-cyclohexane · ligand · chains A
- FE · Fe (III) ion · metal · 2 copies · chains A
- OH · Hydroxide ion · ion · chains A
- FMT · Formic acid · additive · 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 | 81 | 0.74 | 0.98 | 23 | FE, OH, INS |
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 Q9QXN5
- Elsewhere: RCSB PDB 3BXD · PDBe 3BXD · UniProt Q9QXN5
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