Research workbench
Crystal structure of Salmo salar RidA-1
Analyse Crystal structure of Salmo salar RidA-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TCC
- Type
- protein
- Length
- 134 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.05
- Source
- Salmo salar
- Molecule
- ribonuclease UK114
- UniProt
- A0A1S3KNQ3
Structure
x-ray diffraction · resolution 1.05 · 1 distinct chain · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ribonuclease UK114 | protein | 134 | 28% helix, 30% strand | A0A1S3KNQ3 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TCC · Crystal structure of salmo salar rida-1 · 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 A0A1S3KNQ3
- Elsewhere: RCSB PDB 6TCC · PDBe 6TCC · UniProt A0A1S3KNQ3
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