Research workbench
The frpb iron transporter from neisseria meningitidis (F3-3 variant)
Analyse The frpb iron transporter from neisseria meningitidis (F3-3 variant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AIP
- Type
- protein
- Length
- 1,991 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fe-regulated protein B
- UniProt
- Q51162
- Ligands
- N8E, GLU
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fe-regulated protein B | protein | 661 | 8% helix, 53% strand | Q51162 |
| B | Fe-regulated protein B | protein | 665 | 7% helix, 53% strand | Q51162 |
| C | Fe-regulated protein B | protein | 665 | 7% helix, 53% strand | Q51162 |
Ligands and binding sites
- N8E · 3,6,9,12,15-pentaoxatricosan-1-ol · ligand · 2 copies · chains A, C, B
- GLU · Glutamic acid · ligand · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 789 | 0.86 | 0.89 | 103 | empty |
| 2 | 287 | 0.85 | 0.96 | 62 | empty |
| 3 | 235 | 0.84 | 0.96 | 51 | empty |
| 4 | 499 | 0.82 | 0.89 | 61 | empty |
| 5 | 240 | 0.80 | 0.93 | 49 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1181 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 908 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 907 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4AIP · The FrpB iron transporter from Neisseria meningitidis (F3-3 variant) · the same entry in another collection · chain C against C, TM-score 1.00
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 Q51162
- Elsewhere: RCSB PDB 4AIP · PDBe 4AIP · UniProt Q51162
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.