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Structures of P. aeruginosa fpva bound to heterologous pyoverdines: apo-fpva
Analyse Structures of P. aeruginosa fpva bound to heterologous pyoverdines: apo-fpva in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W75
- Type
- protein
- Length
- 1,526 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferripyoverdine receptor
- UniProt
- P48632
- Ligands
- N8E, PO4
- Pockets
- 19 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferripyoverdine receptor | protein | 772 | 8% helix, 56% strand | P48632 |
| B | Ferripyoverdine receptor | protein | 754 | 8% helix, 55% strand | P48632 |
Ligands and binding sites
- N8E · 3,6,9,12,15-pentaoxatricosan-1-ol · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 723 | 0.86 | 0.90 | 101 | PO4 |
| 2 | 488 | 0.85 | 0.92 | 65 | PO4 |
| 3 | 304 | 0.77 | 0.89 | 49 | empty |
| 4 | 1086 | 0.75 | 0.78 | 77 | empty |
| 5 | 1044 | 0.75 | 0.78 | 87 | empty |
Interfaces
1 interface between chains.
- A–B · 657 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2W75 · Structures of P. aeruginosa FpvA bound to heterologous pyoverdines: Apo-FpvA · the same entry in another collection · chain A against A, TM-score 1.00
- P48632 · AlphaFold monomer V2.0 prediction for ferripyoverdine receptor (P48632) · a predicted model of the same protein · chain A against A, 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 P48632
- Elsewhere: RCSB PDB 2W75 · PDBe 2W75 · UniProt P48632
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