SIGNAL RECOGNITION PARTICLE 9/14 FUSION PROTEIN
Mus musculus
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 1–110 | Fragment：ALU RNA BINDING HETERODIMER | PO4 PHOSPHATE ION × 1 BME BETA-MERCAPTOETHANOL × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：hanging drop；pH 7.7；277 K；THE SRPPHI14-9 PROTEIN WAS CRYSTALLIZED (BIRSE ET AL., FEBS LETTERS, 1996) BY THE HANGING DROP METHOD IN 2.0 M NAH2/K2H PO4, PH 7.7, 2% MPD, 1.0 MM NAN3 AT 4 DEGREES C WITH A FINAL PROTEIN CONCENTRATION OF 5-8 MG ML-1. CRYSTALS FORMED OVER 2-3 WEEKS AND WERE TYPICALLY 150 X 150 X 300 MM3 IN SPACE, hanging drop, temperature 277K | Resolution 2.53 Å R-free 0.299 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
No other PDB entry for the same UniProt protein was found.
View Construct and Data Evidence
| UniProt name | SR14_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 20–129； UniProt 1–110 |
