Research workbench
Structural insight into G protein coupling and regulation of FE2+ membrane transport
Analyse Structural insight into G protein coupling and regulation of FE2+ membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HYR
- Type
- protein
- Length
- 759 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrous iron transport protein B
- UniProt
- P33650
- Pockets
- 12 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Ferrous iron transport protein B | protein | 253 | 51% helix, 17% strand | P33650 |
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 316 | 0.65 | 0.81 | 33 | empty |
| 2 | 314 | 0.64 | 0.80 | 30 | empty |
| 3 | 333 | 0.64 | 0.79 | 32 | empty |
| 4 | 392 | 0.58 | 0.75 | 59 | empty |
| 5 | 220 | 0.57 | 0.79 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–C · 717 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 716 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 715 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3HYR · Structural Insight into G Protein Coupling and Regulation of Fe2+ Membrane Transport · 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 A 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 3HYR · PDBe 3HYR · UniProt P33650
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