Research workbench
Crystal structure of fosfomycin resistance protein fosx from mesorhizobium loti
Analyse Crystal structure of fosfomycin resistance protein fosx from mesorhizobium loti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R9C
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase
- EC
- 2.5.1.1
- UniProt
- Q98GG1
- Ligands
- MN
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione transferase (EC 2.5.1.1) | protein | 125 | 28% helix, 36% strand | Q98GG1 |
| B | Glutathione transferase (EC 2.5.1.1) | protein | 118 | 25% helix, 36% strand | Q98GG1 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.80 | 0.97 | 23 | empty |
| 2 | 82 | 0.44 | 0.80 | 20 | empty |
| 3 | 91 | 0.39 | 0.76 | 18 | MN |
Interfaces
1 interface between chains.
- A–B · 1906 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 1R9C · Crystal Structure of Fosfomycin Resistance Protein FosX from Mesorhizobium Loti · the same entry in another collection · chain A against A, TM-score 1.00
- Q98GG1 · AlphaFold monomer V2.0 prediction for fosfomycin resistance protein fosx (Q98GG1) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q98GG1
- Elsewhere: RCSB PDB 1R9C · PDBe 1R9C · UniProt Q98GG1
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