7n9z

E. coli cytochrome bo3 in MSP nanodisc

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytochrome o ubiquinol oxidase, subunit I

OrganismNot specified

UniProt H4KCU1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Ubiquinol oxidase subunit 2 × 1 (A0A024L5V9) Cytochrome o ubiquinol oxidase × 1 (D6I7E4) Cytochrome o ubiquinol oxidase, subunit IV × 1 (I2RK84) Ubiquinone-8 × 1 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEME O × 1 PROTOPORPHYRIN IX CONTAINING FE × 1 CARDIOLIPIN × 1 COPPER (II) ION × 1 ZINC ION × 1 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H4KCU1_ECOLX
Isoform —
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–663; UniProt 1–663

Ubiquinol oxidase subunit 2

OrganismNot specified

UniProt A0A024L5V9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Cytochrome o ubiquinol oxidase, subunit I × 1 (H4KCU1) Cytochrome o ubiquinol oxidase × 1 (D6I7E4) Cytochrome o ubiquinol oxidase, subunit IV × 1 (I2RK84) Ubiquinone-8 × 1 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEME O × 1 PROTOPORPHYRIN IX CONTAINING FE × 1 CARDIOLIPIN × 1 COPPER (II) ION × 1 ZINC ION × 1 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A024L5V9_ECOLX
Isoform —
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–315; UniProt 1–315

Cytochrome o ubiquinol oxidase

OrganismNot specified

UniProt D6I7E4

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Cytochrome o ubiquinol oxidase, subunit I × 1 (H4KCU1) Ubiquinol oxidase subunit 2 × 1 (A0A024L5V9) Cytochrome o ubiquinol oxidase, subunit IV × 1 (I2RK84) Ubiquinone-8 × 1 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEME O × 1 PROTOPORPHYRIN IX CONTAINING FE × 1 CARDIOLIPIN × 1 COPPER (II) ION × 1 ZINC ION × 1 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name D6I7E4_ECOLX
Isoform —
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–204; UniProt 1–204

Cytochrome o ubiquinol oxidase, subunit IV

OrganismNot specified

UniProt I2RK84

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Cytochrome o ubiquinol oxidase, subunit I × 1 (H4KCU1) Ubiquinol oxidase subunit 2 × 1 (A0A024L5V9) Cytochrome o ubiquinol oxidase × 1 (D6I7E4) Ubiquinone-8 × 1 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEME O × 1 PROTOPORPHYRIN IX CONTAINING FE × 1 CARDIOLIPIN × 1 COPPER (II) ION × 1 ZINC ION × 1 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name I2RK84_ECOLX
Isoform —
PDB entities 4
Chains and sequence ranges Author chain I; PDBConstruct 1–109; UniProt 1–109

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id7n9z
Deposition date deposition_date2021-06-19
Structure title titleE. coli cytochrome bo3 in MSP nanodisc
Keywords keywordsUbiquinone, Heme-copper Oxidoreductase, Electron transport, Bioenergetics, Proton pump, Membrane protein; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7n9z__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7n9z__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7n9z__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)32.43 Å
Rg (electron density)30.91 Å
Total Rg31.72 Å
Atom count20611
Residues1202
Excluded volume188710 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7n9z__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (13)

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7. Citations (1)