Research workbench
Crystal structure of ferric reductase from archaeoglobus fulgidus
Analyse Crystal structure of ferric reductase from archaeoglobus fulgidus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I0R
- Type
- protein
- Length
- 329 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein
- UniProt
- O29428
- Ligands
- FMN
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved hypothetical protein | protein | 161 | 19% helix, 45% strand | O29428 |
| B | Conserved hypothetical protein | protein | 168 | 23% helix, 45% strand | O29428 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 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 | 1146 | 0.74 | 0.77 | 101 | FMN |
Interfaces
1 interface between chains.
- A–B · 2264 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 1I0R · Crystal structure of ferric reductase from archaeoglobus fulgidus · the same entry in another collection · chain A against A, TM-score 1.00
- O29428 · AlphaFold monomer V2.0 prediction for ferric-chelate reductase (NAD(P)H) (O29428) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O29428
- Elsewhere: RCSB PDB 1I0R · PDBe 1I0R · UniProt O29428
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