Structures of SRP54 and SRP19, the two proteins assembling the ribonucleic core of the signal recognition particle from the archaeon pyrococcus furiosus.

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 27% strand (DSSP).

Ligands and binding sites

• BR · Bromide ion · ion · 39 copies · chains A, B, C, D
• MLI · Malonate ion · additive · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• C–D · 700 Ų buried · 5 hydrogen bonds · protein-protein
• A–B · 676 Ų buried · 4 hydrogen bonds · protein-protein
• B–C · 494 Ų buried · 18 hydrogen bonds · protein-protein
• A–D · 467 Ų buried · 18 hydrogen bonds · protein-protein
• B–D · 168 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 3DLU · Structures of SRP54 and SRP19, the two proteins assembling the ribonucleic core of the… · the same entry in another collection · chain D against D, TM-score 1.00
• Q8TZT9 · AlphaFold monomer V2.0 prediction for signal recognition particle 19 kda protein (Q8TZT9) · a predicted model of the same protein · chain D against A, TM-score 0.93

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 Q8TZT9
• Elsewhere: RCSB PDB 3DLU · PDBe 3DLU · UniProt Q8TZT9