Chloramphenicol O-acetyltransferase
Bacteroides uniformis dnLKV2
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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count | Chain A； UniProt 1–219 Chain B； UniProt 1–219 Chain C； UniProt 1–219 | Not recorded | BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 SO4 SULFATE ION × 2 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M BIS-TRIS pH 6.5, 25% w/v Polyethylene glycol 3,350 | Resolution 1.59 Å R-free 0.209 |
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 | R9HWB4_BACUN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–220； UniProt 1–219 Author chain B； PDBConstruct 2–220； UniProt 1–219 Author chain C； PDBConstruct 2–220； UniProt 1–219 |
