Peptidyl-prolyl cis-trans isomerase
Brugia malayi
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 1–171 | Mutation：K5H, S166A | SO4 SULFATE ION × 3 CL CHLORIDE ION × 3 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；Index A5: 2.0 M Ammonium sulfate, 0.1 M HEPES pH 7.5. BrmaA.01375.b.B1.PS01744 at 31 mg/mL. plate 14177 A4 drop 2, Puck: BNL-OEP 001-008, Cryo: 80% crystallant + 20% PEG 200 | Resolution 1.25 Å R-free 0.135 |
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 | A0A0J9XUF2_BRUMA |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 9–179； UniProt 1–171 |
