Research workbench
Structure of the cytosolic domain of E. COLI feob, nucleotide-free form
Analyse Structure of the cytosolic domain of E. COLI feob, nucleotide-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I8S
- Type
- protein
- Length
- 782 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrous iron transport protein B
- UniProt
- P33650
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrous iron transport protein B | protein | 260 | 52% helix, 18% strand | P33650 |
| B, C | Ferrous iron transport protein B | protein | 261 | 50% helix, 17% strand | P33650 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.79 | 0.80 | 81 | empty |
| 2 | 895 | 0.77 | 0.80 | 85 | empty |
| 3 | 340 | 0.63 | 0.79 | 42 | empty |
| 4 | 92 | 0.43 | 0.79 | 16 | empty |
| 5 | 94 | 0.42 | 0.78 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 761 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 598 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 174 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3I8S · Structure of the cytosolic domain of E. coli FeoB, nucleotide-free form · the same entry in another collection · chain A against A, TM-score 1.00
- P33650 · AlphaFold monomer V2.0 prediction for FE(2+) transporter feob (P33650) · 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 P33650
- Elsewhere: RCSB PDB 3I8S · PDBe 3I8S · UniProt P33650
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