7xmd

Cryo-EM structure of Cytochrome bo3 from Escherichia coli, the structure complexed with an allosteric inhibitor N4

Method: ELECTRON MICROSCOPY

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytochrome bo(3) ubiquinol oxidase subunit 1

Escherichia coli

UniProt P0ABI8

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–663 Not recorded Ubiquinol oxidase subunit 2 × 1 (A0A024L5V9) Cytochrome bo(3) ubiquinol oxidase subunit 3 × 1 (P0ABJ3) Cytochrome bo(3) ubiquinol oxidase subunit 4 × 1 (P0ABJ6) HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CU COPPER (II) ION × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 JYR methyl 3-oxidanyl-5-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-1-benzothiophene-2-carboxylate × 1 UNX UNKNOWN LIGAND × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 Å

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.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

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

Ubiquinol oxidase subunit 2

Escherichia coli

UniProt A0A024L5V9

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–315 Not recorded Cytochrome bo(3) ubiquinol oxidase subunit 1 × 1 (P0ABI8) Cytochrome bo(3) ubiquinol oxidase subunit 3 × 1 (P0ABJ3) Cytochrome bo(3) ubiquinol oxidase subunit 4 × 1 (P0ABJ6) HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CU COPPER (II) ION × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 JYR methyl 3-oxidanyl-5-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-1-benzothiophene-2-carboxylate × 1 UNX UNKNOWN LIGAND × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

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

Cytochrome bo(3) ubiquinol oxidase subunit 3

Escherichia coli

UniProt P0ABJ3

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–204 Not recorded Cytochrome bo(3) ubiquinol oxidase subunit 1 × 1 (P0ABI8) Ubiquinol oxidase subunit 2 × 1 (A0A024L5V9) Cytochrome bo(3) ubiquinol oxidase subunit 4 × 1 (P0ABJ6) HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CU COPPER (II) ION × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 JYR methyl 3-oxidanyl-5-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-1-benzothiophene-2-carboxylate × 1 UNX UNKNOWN LIGAND × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 Å

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.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

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

Cytochrome bo(3) ubiquinol oxidase subunit 4

Escherichia coli

UniProt P0ABJ6

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–109 Not recorded Cytochrome bo(3) ubiquinol oxidase subunit 1 × 1 (P0ABI8) Ubiquinol oxidase subunit 2 × 1 (A0A024L5V9) Cytochrome bo(3) ubiquinol oxidase subunit 3 × 1 (P0ABJ3) HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CU COPPER (II) ION × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 JYR methyl 3-oxidanyl-5-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-1-benzothiophene-2-carboxylate × 1 UNX UNKNOWN LIGAND × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYOD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; 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.

SAXS scattering curve SAXS Profile

暂无 SAXS 图

P(r) Distance Distribution P(r) Distribution

暂无 P(r) 图
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7xmd
Deposition date deposition_date2022-04-25
Structure title titleCryo-EM structure of Cytochrome bo3 from Escherichia coli, the structure complexed with an allosteric inhibitor N4
Keywords keywordsrespiratory enzyme, membrane protein, heme protein, allosteric inhibitor, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

该条目暂无 SAXS 数据。

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

该条目暂无 P(r) 分析数据。

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (0)