7au3

Cytochrome c oxidase structure in F-state

Method: ELECTRON MICROSCOPY

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

Cytochrome c oxidase subunit 1-beta

OrganismNot specified

UniProt P98002

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 1–558 Not recorded Cytochrome c oxidase subunit 2 × 1 (P08306) Cytochrome c oxidase subunit 3 × 1 (P06030) Cytochrome c oxidase subunit 4 × 1 (P77921) MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 O OXYGEN ATOM × 1 2FK SUPEROXO ION × 1 CUA DINUCLEAR COPPER ION × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4 seconds before plunging Resolution 2.56 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 COX1B_PARDE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–558; UniProt 1–558

Cytochrome c oxidase subunit 2

OrganismNot specified

UniProt P08306

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 1–298 Not recorded Cytochrome c oxidase subunit 1-beta × 1 (P98002) Cytochrome c oxidase subunit 3 × 1 (P06030) Cytochrome c oxidase subunit 4 × 1 (P77921) MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 O OXYGEN ATOM × 1 2FK SUPEROXO ION × 1 CUA DINUCLEAR COPPER ION × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4 seconds before plunging Resolution 2.56 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 COX2_PARDE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–298; UniProt 1–298

Cytochrome c oxidase subunit 3

OrganismNot specified

UniProt P06030

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 1–274 Not recorded Cytochrome c oxidase subunit 1-beta × 1 (P98002) Cytochrome c oxidase subunit 2 × 1 (P08306) Cytochrome c oxidase subunit 4 × 1 (P77921) MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 O OXYGEN ATOM × 1 2FK SUPEROXO ION × 1 CUA DINUCLEAR COPPER ION × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4 seconds before plunging Resolution 2.56 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX3_PARDE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–274; UniProt 1–274

Cytochrome c oxidase subunit 4

OrganismNot specified

UniProt P77921

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 1–50 Not recorded Cytochrome c oxidase subunit 1-beta × 1 (P98002) Cytochrome c oxidase subunit 2 × 1 (P08306) Cytochrome c oxidase subunit 3 × 1 (P06030) MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 O OXYGEN ATOM × 1 2FK SUPEROXO ION × 1 CUA DINUCLEAR COPPER ION × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4 seconds before plunging Resolution 2.56 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX4_PARDE
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–50; UniProt 1–50

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_id7au3
Deposition date deposition_date2020-11-02
Structure title titleCytochrome c oxidase structure in F-state
Keywords keywordsTerminal oxidase Cytochrome c oxidase aa3 oxidase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
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 (13)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7au3A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology210 — Cytochrome C Oxidase; Chain A
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase-like, subunit I domain

8. Citations (1)

9. Files and Curves (0)