Research workbench
Crystal structure of the read-through domain from bacteriophage qbeta A1 protein, monoclinic crystal form
Analyse Crystal structure of the read-through domain from bacteriophage qbeta A1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RLK
- Type
- protein
- Length
- 183 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- A1 protein
- UniProt
- Q8LTE1
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A1 protein | protein | 183 | 15% helix, 32% strand | Q8LTE1 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3RLK · Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein… · 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 Q8LTE1
- Elsewhere: RCSB PDB 3RLK · PDBe 3RLK · UniProt Q8LTE1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.