Research workbench
Crystal structure of the reduced form of oxyr
Analyse Crystal structure of the reduced form of oxyr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I69
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrogen peroxide-inducible genes activator
- UniProt
- P0ACQ4
- Ligands
- BEZ
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrogen peroxide-inducible genes activator | protein | 206 | 31% helix, 29% strand | P0ACQ4 |
| B | Hydrogen peroxide-inducible genes activator | protein | 206 | 30% helix, 30% strand | P0ACQ4 |
Ligands and binding sites
- BEZ · Benzoic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.76 | 0.79 | 65 | BEZ |
| 2 | 182 | 0.68 | 0.86 | 24 | empty |
| 3 | 76 | 0.35 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1134 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1I69 · Crystal structure of the reduced form of oxyr · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACQ4 · AlphaFold monomer V2.0 prediction for hydrogen peroxide-inducible genes activator (P0ACQ4) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P0ACQ4
- Elsewhere: RCSB PDB 1I69 · PDBe 1I69 · UniProt P0ACQ4
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