Serine/threonine-protein kinase
Trypanosoma brucei brucei TREU927
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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain A； UniProt 54–406 Chain B； UniProt 54–406 | Fragment：residues 54-406 Non-standard monomer：Yes (specific site not provided by mmCIF) Fragment：residues 54-406 | SO4 SULFATE ION × 11 CL CHLORIDE ION × 10 GOL GLYCEROL × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；291 K；IDX G2 (25% (w/v) PEG 3350, 0.1 M BIS-TRIS pH 5.5, 0.2 M lithium sulfate. TrbrA.01480.a.WW4.PS38793 at 13.5 mg/mL. The C-terminal tail ~60 residues was disordered in each subunit. Residue Ser 71 in subunit A contained a large amount of density near the OG atom. This was modeled as a phosphoserine (SEP) although this is not a predicted phosphorylation site. plate 20520 G2 drop 1, Puck: PSL-0604, Cryo: 80% crystallant + 20% glycerol | Resolution 2.05 Å R-free 0.235 |
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.
1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | Q582V7_TRYB2 |
| Isoform | — |
| PDB entities | 1, 2 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–354； UniProt 54–406 Author chain B； PDBConstruct 2–354； UniProt 54–406 |
