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Crystal strutcure of the fosfomycin resistance protein a (fosa) containing bound thallium cations
Analyse Crystal strutcure of the fosfomycin resistance protein a (fosa) containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LQO
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable fosfomycin resistance protein
- EC
- 2.5.1.18
- UniProt
- Q9I4K6
- Ligands
- TL, MN, PO4
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable fosfomycin resistance protein (EC 2.5.1.18) | protein | 134 | 25% helix, 38% strand | Q9I4K6 |
Ligands and binding sites
- TL · Thallium (I) ion · metal · 6 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.67 | 0.95 | 21 | empty |
| 2 | 149 | 0.58 | 0.83 | 23 | PO4, TL |
| 3 | 107 | 0.50 | 0.81 | 23 | PO4, MN, TL |
| 4 | 53 | 0.32 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2660 Ų buried · 48 hydrogen bonds · protein-protein
Compared structures
- 1LQO · Crystal Strutcure of the Fosfomycin Resistance Protein A (FosA) Containing Bound Thallium… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9I4K6 · AlphaFold monomer V2.0 prediction for glutathione transferase fosa (Q9I4K6) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9I4K6
- Elsewhere: RCSB PDB 1LQO · PDBe 1LQO · UniProt Q9I4K6
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