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Crystal structure of T. acidophilum IdeR
Analyse Crystal structure of T. acidophilum IdeR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O5V
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Thermoplasma acidophilum
- Molecule
- Iron-dependent transcription repressor related protein
- UniProt
- Q9HJU1
- Ligands
- FE2
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Iron-dependent transcription repressor related protein | protein | 213 | 46% helix, 21% strand | Q9HJU1 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.56 | 0.81 | 20 | empty |
| 2 | 104 | 0.42 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 4O5V · Crystal structure of T. acidophilum ider · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9HJU1
- Elsewhere: RCSB PDB 4O5V · PDBe 4O5V · UniProt Q9HJU1
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