Current Protein Identity:H4KCU1 New Search
Main Difference Dimensions in This Set
Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
6WTI The Cryo-EM structure of the ubiquinol oxidase from Escherichia coli Deposited 2020-05-02 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–663(663 aa)
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEO HEME O × 1 CU COPPER (II) ION × 1 UQ8 Ubiquinone-8 × 1 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 9 U9V pentadecyl(tetradecyl)peroxyanhydride × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.38 Å
7N9Z E. coli cytochrome bo3 in MSP nanodisc Deposited 2021-06-19 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain F 1–663(663 aa)
Not recorded UQ8 Ubiquinone-8 × 1 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CDL CARDIOLIPIN × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.19 Å