Research workbench
Structure of QNRB1 (M102R-trypsin treated), a plasmid-mediated fluoroquinolone resistance protein
Analyse Structure of QNRB1 (M102R-trypsin treated), a plasmid-mediated fluoroquinolone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XTX
- Type
- protein
- Length
- 420 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- QNRB1
- UniProt
- Q2I1Y8
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | QNRB1 | protein | 207 | 4% helix, 27% strand | Q2I1Y8 |
| B | QNRB1 | protein | 213 | 4% helix, 29% strand | Q2I1Y8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 833 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2XTX · Structure of QnrB1 (M102R-Trypsin Treated), a plasmid-mediated fluoroquinolone resistance… · the same entry in another collection · 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 Q2I1Y8
- Elsewhere: RCSB PDB 2XTX · PDBe 2XTX · UniProt Q2I1Y8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.