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1qle

CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT

Method: X-RAY DIFFRACTION Dmax: 125.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CYTOCHROME C OXIDASE POLYPEPTIDE I-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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain A； UniProt 17–554 Not recorded CYTOCHROME C OXIDASE POLYPEPTIDE II × 1 （P08306） CYTOCHROME C OXIDASE POLYPEPTIDE III × 1 （P06030） CCYTOCHROME C OXIDASE × 1 （P77921） HEAVY CHAIN ANTIBODY FV FRAGMENT × 1 LIGHT CHAIN ANTIBODY FV FRAGMENT × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.00 Resolution 3.00 Å R-free 0.309

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.

Other PDB Difference from Current Entry 1QLE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AR1 Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment Deposited 1997-08-08 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa）
Not recorded CU COPPER (II) ION × 3 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 HEA HEME-A × 2 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 9 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；pH 5.5
Resolution 2.70 Å R-free 0.261
3EHB A D-Pathway Mutation Decouples the Paracoccus Denitrificans Cytochrome c Oxidase by Altering the side chain orientation of a distant, conserved Glutamate Deposited 2008-09-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa） Fragment：UNP residues 17-545
Mutation：N131D HEA HEME-A × 2 CU COPPER (II) ION × 3 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 9 LMT DODECYL-BETA-D-MALTOSIDE × 12 PER PEROXIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；291 K；MPEG 2000 is contained in the crystallization buffer pH 5.5, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.32 Å R-free 0.242
3HB3 High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase Deposited 2009-05-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa）
Not recorded HEA HEME-A × 2 CU1 COPPER (I) ION × 3 MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 10 LMT DODECYL-BETA-D-MALTOSIDE × 14 PEO HYDROGEN PEROXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；277 K；25% glycerol, pH 5.5, VAPOR DIFFUSION, temperature 277K
Resolution 2.25 Å R-free 0.280
7ATE Cytochrome c oxidase structure in P-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 PEO HYDROGEN PEROXIDE × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 second before plunging
Resolution 2.40 Å
7ATN Cytochrome c oxidase structure in R-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.66 Å
7AU3 Cytochrome c oxidase structure in F-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa）
Not recorded 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
7AU6 Cytochrome c oxidase structure in O-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–558（558 aa）
Not recorded HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 OXY OXYGEN MOLECULE × 6 PEO HYDROGEN PEROXIDE × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.40 Å

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

View Construct and Data Evidence
UniProt name CX1B_PARDE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–538； UniProt 17–554

CYTOCHROME C OXIDASE POLYPEPTIDE II

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain B； UniProt 30–281 Not recorded CYTOCHROME C OXIDASE POLYPEPTIDE I-BETA × 1 （P98002） CYTOCHROME C OXIDASE POLYPEPTIDE III × 1 （P06030） CCYTOCHROME C OXIDASE × 1 （P77921） HEAVY CHAIN ANTIBODY FV FRAGMENT × 1 LIGHT CHAIN ANTIBODY FV FRAGMENT × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.00 Resolution 3.00 Å R-free 0.309

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.

Other PDB Difference from Current Entry 1QLE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AR1 Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment Deposited 1997-08-08 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded CU COPPER (II) ION × 3 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 HEA HEME-A × 2 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 9 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；pH 5.5
Resolution 2.70 Å R-free 0.261
3EHB A D-Pathway Mutation Decouples the Paracoccus Denitrificans Cytochrome c Oxidase by Altering the side chain orientation of a distant, conserved Glutamate Deposited 2008-09-12 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded HEA HEME-A × 2 CU COPPER (II) ION × 3 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 9 LMT DODECYL-BETA-D-MALTOSIDE × 12 PER PEROXIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；291 K；MPEG 2000 is contained in the crystallization buffer pH 5.5, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.32 Å R-free 0.242
3HB3 High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase Deposited 2009-05-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded HEA HEME-A × 2 CU1 COPPER (I) ION × 3 MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 10 LMT DODECYL-BETA-D-MALTOSIDE × 14 PEO HYDROGEN PEROXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；277 K；25% glycerol, pH 5.5, VAPOR DIFFUSION, temperature 277K
Resolution 2.25 Å R-free 0.280
7ATE Cytochrome c oxidase structure in P-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 PEO HYDROGEN PEROXIDE × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 second before plunging
Resolution 2.40 Å
7ATN Cytochrome c oxidase structure in R-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.66 Å
7AU3 Cytochrome c oxidase structure in F-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded 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
7AU6 Cytochrome c oxidase structure in O-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–298（298 aa）
Not recorded HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 OXY OXYGEN MOLECULE × 6 PEO HYDROGEN PEROXIDE × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.40 Å

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 1–252； UniProt 30–281

CYTOCHROME C OXIDASE POLYPEPTIDE III

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain C； UniProt 1–273 Not recorded CYTOCHROME C OXIDASE POLYPEPTIDE I-BETA × 1 （P98002） CYTOCHROME C OXIDASE POLYPEPTIDE II × 1 （P08306） CCYTOCHROME C OXIDASE × 1 （P77921） HEAVY CHAIN ANTIBODY FV FRAGMENT × 1 LIGHT CHAIN ANTIBODY FV FRAGMENT × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.00 Resolution 3.00 Å R-free 0.309

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.

Other PDB Difference from Current Entry 1QLE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7ATE Cytochrome c oxidase structure in P-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–274（274 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 PEO HYDROGEN PEROXIDE × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 second before plunging
Resolution 2.40 Å
7ATN Cytochrome c oxidase structure in R-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–274（274 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.66 Å
7AU3 Cytochrome c oxidase structure in F-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–274（274 aa）
Not recorded 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
7AU6 Cytochrome c oxidase structure in O-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–274（274 aa）
Not recorded HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 OXY OXYGEN MOLECULE × 6 PEO HYDROGEN PEROXIDE × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.40 Å

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 1–273； UniProt 1–273

CCYTOCHROME C OXIDASE

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain D； UniProt 8–50 Not recorded CYTOCHROME C OXIDASE POLYPEPTIDE I-BETA × 1 （P98002） CYTOCHROME C OXIDASE POLYPEPTIDE II × 1 （P08306） CYTOCHROME C OXIDASE POLYPEPTIDE III × 1 （P06030） HEAVY CHAIN ANTIBODY FV FRAGMENT × 1 LIGHT CHAIN ANTIBODY FV FRAGMENT × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.00 Resolution 3.00 Å R-free 0.309

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.

Other PDB Difference from Current Entry 1QLE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7ATE Cytochrome c oxidase structure in P-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 1–50（50 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 PEO HYDROGEN PEROXIDE × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 second before plunging
Resolution 2.40 Å
7ATN Cytochrome c oxidase structure in R-state Deposited 2020-10-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 1–50（50 aa）
Not recorded MN MANGANESE (II) ION × 1 HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.66 Å
7AU3 Cytochrome c oxidase structure in F-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 1–50（50 aa）
Not recorded 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
7AU6 Cytochrome c oxidase structure in O-state Deposited 2020-11-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 1–50（50 aa）
Not recorded HEA HEME-A × 2 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 OXY OXYGEN MOLECULE × 6 PEO HYDROGEN PEROXIDE × 1 MN MANGANESE (II) ION × 1 CUA DINUCLEAR COPPER ION × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；4 seconds before plunging
Resolution 2.40 Å

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

View Construct and Data Evidence
UniProt name P77921
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D； PDBConstruct 1–43； UniProt 8–50

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

SAXS profile for 1qle

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qle
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qle
Deposition date deposition_date1999-08-30
Structure title titleCRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT
Keywords keywords;OXIDOREDUCTASE/IMMUNE SYSTEM, COMPLEX (OXIDOREDUCTASE-ANTIBODY), ELECTRON TRANSPORT, TRANSMEMBRANE, CYTOCHROME OXIDASE, ANTIBODY COMPLEX, OXIDOREDUCTASE-IMMUNE SYSTEM complex ;; OXIDOREDUCTASE/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier36.90 Å
Radius of gyration Rg (electron density) rg_electron36.08 Å
Forward intensity I(0) i0295668000.00
Molecular weight molecular_weight152290.0 kDa
Excluded volume excluded_volume195180 ų
Envelope volume envelope_volume232040 ų
Hydration-shell volume shell_volume53873 ų
Envelope diameter envelope_diameter130.3 Å
Shell Rg shell_rg42.27 Å
Envelope Rg envelope_rg36.44 Å
Shape Rg shape_rg36.07 Å
Total Rg total_rg36.53 Å
Total atoms total_atoms10762
Residues n_residues1333
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax125.6 Å
Rg (real space) rg_real37.04 Å
Rg uncertainty (real space) rg_real_error0.93 Å
I(0) (real space) i0_real2.9570e+08
I(0) uncertainty (real space) i0_real_error4.2520e+06
Rg (reciprocal space) rg_reciprocal36.96 Å
I(0) (reciprocal space) i0_reciprocal295600000.0000
Solution quality estimate total_estimate0.8616
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.9 Å
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.253
Angular range angular_range— – 0.2150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60330000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.812
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (12)

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7. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1qlea_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.24 — Cytochrome c oxidase subunit I-like
Superfamily Superfamily superfamilyf.24.1 — Cytochrome c oxidase subunit I-like
Family Family familyf.24.1.1 — Cytochrome c oxidase subunit I-like
Domain ID domain_idd1qleb1
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.2 — Periplasmic domain of cytochrome c oxidase subunit II
Domain ID domain_idd1qleb2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.2 — Cytochrome c oxidase subunit II-like, transmembrane region
Family Family familyf.17.2.1 — Cytochrome c oxidase subunit II-like, transmembrane region
Domain ID domain_idd1qlec_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.25 — Cytochrome c oxidase subunit III-like
Superfamily Superfamily superfamilyf.25.1 — Cytochrome c oxidase subunit III-like
Family Family familyf.25.1.1 — Cytochrome c oxidase subunit III-like
Domain ID domain_idd1qled_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.8 — Bacterial aa3 type cytochrome c oxidase subunit IV
Family Family familyf.23.8.1 — Bacterial aa3 type cytochrome c oxidase subunit IV
Domain ID domain_idd1qleh_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1qlel_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (8 domains)

Domain ID domain_id1qleA00
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
Domain ID domain_id1qleB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1qleB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily90 —
Domain ID domain_id1qleC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70 —
Domain ID domain_id1qleC02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily80 — Cytochrome c oxidase, subunit III, four-helix bundle
Domain ID domain_id1qleD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily160 — Bacterial aa3 type cytochrome c oxidase subunit IV
Domain ID domain_id1qleH00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1qleL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
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8. Citations (1)

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9. Files and Curves (10)