Research workbench
Moonlighting functions of feoc in the regulation of ferrous iron transport in feo
Analyse Moonlighting functions of feoc in the regulation of ferrous iron transport in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AWX
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrous iron transport protein B; Ferrous iron transport protein C
- UniProt
- C4X1R9, B5XTS6
- Ligands
- NI, SO4
- Pockets
- 4 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrous iron transport protein B | protein | 252 | 46% helix, 18% strand | C4X1R9 |
| B | Ferrous iron transport protein C | protein | 63 | 51% helix, 17% strand | B5XTS6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.44 | 0.81 | 12 | empty |
| 2 | 67 | 0.36 | 0.78 | 15 | empty |
| 3 | 53 | 0.32 | 0.77 | 20 | empty |
| 4 | 50 | 0.27 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 926 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4AWX · Moonlighting functions of FeoC in the regulation of ferrous iron transport in Feo · the same entry in another collection · chain A against A, TM-score 1.00
- B5XTS6 · AlphaFold monomer V2.0 prediction for probable [fe-S]-dependent transcriptional repressor… · a predicted model of the same protein · chain B against A, TM-score 0.89
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 C4X1R9
- Every structure of UniProt B5XTS6
- Elsewhere: RCSB PDB 4AWX · PDBe 4AWX · UniProt C4X1R9 · UniProt B5XTS6
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