Research workbench
Structure of the macrocycle thiostrepton solved using the anomalous dispersive contribution from sulfur
Analyse Structure of the macrocycle thiostrepton solved using the anomalous dispersive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E9W
- Type
- protein
- Length
- 17 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0C8P8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 17 | — | P0C8P8 |
Compared structures
- 1E9W · Structure of the macrocycle thiostrepton solved using the anomalous dispersive… · the same entry in another collection · chain A against A, TM-score 1.00
- 1OLN · Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA · a predicted model of the same protein · chain A against B, TM-score 1.00
- 1OLN · Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA · a predicted model of the same protein · chain A against B, TM-score 1.00
- P0C8P8 · AlphaFold monomer V2.0 prediction for thiostrepton (P0C8P8) · a predicted model of the same protein · chain A against A, TM-score 0.12
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 P0C8P8
- Elsewhere: RCSB PDB 1E9W · PDBe 1E9W · UniProt P0C8P8
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