Research workbench
Structural basis for the iron uptake mechanism of helicobacter pylori ferritin
Analyse Structural basis for the iron uptake mechanism of helicobacter pylori ferritin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BVI
- Type
- protein
- Length
- 1,033 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- EC
- 1.16.3.1
- UniProt
- Q9ZLI1
- Ligands
- FE
- Pockets
- 11 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Ferritin (EC 1.16.3.1) | protein | 172 | 76% helix, 1% strand | Q9ZLI1 |
| F | Ferritin (EC 1.16.3.1) | protein | 173 | 76% helix, 1% strand | Q9ZLI1 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 15 copies · chains A, B, D, C, E, F
- GOL · Glycerol · additive · 3 copies · chains C, D, B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.54 | 0.76 | 35 | empty |
| 2 | 213 | 0.50 | 0.76 | 27 | empty |
| 3 | 131 | 0.48 | 0.79 | 24 | empty |
| 4 | 132 | 0.47 | 0.78 | 23 | empty |
| 5 | 72 | 0.43 | 0.81 | 14 | empty |
Interfaces
8 interfaces between chains.
- C–D · 1429 Ų buried · 10 hydrogen bonds · protein-protein
- A–F · 1418 Ų buried · 13 hydrogen bonds · protein-protein
- B–E · 1400 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 816 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 815 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3BVI · Structural basis for the iron uptake mechanism of Helicobacter pylori ferritin · the same entry in another collection · chain F against F, TM-score 1.00
- Q9ZLI1 · AlphaFold monomer V2.0 prediction for bacterial non-heme ferritin (Q9ZLI1) · a predicted model of the same protein · chain F against A, TM-score 0.96
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 Q9ZLI1
- Elsewhere: RCSB PDB 3BVI · PDBe 3BVI · UniProt Q9ZLI1
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