Assemblies
Multimeric state:
hetero octadecamer
Accessible surface area:
85767.82 Å2
Buried surface area:
80787.77 Å2
Dissociation area:
2,750.19
Å2
Dissociation energy (ΔGdiss):
17.43
kcal/mol
Dissociation entropy (TΔSdiss):
19.94
kcal/mol
Symmetry number:
2
PDBe Complex ID:
PDB-CPX-275746
Macromolecules
Chains: A, I
Length: 215 amino acids
Theoretical weight: 24.19 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: Cytochrome b/b6/petB
Length: 215 amino acids
Theoretical weight: 24.19 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P00165 (Residues: 1-215; Coverage: 100%)
Pfam: Cytochrome b/b6/petB
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P00165
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: B, J
Length: 160 amino acids
Theoretical weight: 17.46 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: Cytochrome b(C-terminal)/b6/petD
Length: 160 amino acids
Theoretical weight: 17.46 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P00166 (Residues: 1-160; Coverage: 100%)
Pfam: Cytochrome b(C-terminal)/b6/petD
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P00166
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: C, K
Length: 320 amino acids
Theoretical weight: 35.36 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam:
Length: 320 amino acids
Theoretical weight: 35.36 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P16013 (Residues: 1-320; Coverage: 100%)
Pfam:
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P16013
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: D, L
Length: 230 amino acids
Theoretical weight: 24.35 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: Rieske [2Fe-2S] domain
Length: 230 amino acids
Theoretical weight: 24.35 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P08980 (Residues: 1-230; Coverage: 100%)
Pfam: Rieske [2Fe-2S] domain
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P08980
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: E, M
Length: 31 amino acids
Theoretical weight: 3.45 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: Cytochrome B6-F complex subunit VI (PetL)
Length: 31 amino acids
Theoretical weight: 3.45 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
Q9M3L0 (Residues: 1-31; Coverage: 100%)
Pfam: Cytochrome B6-F complex subunit VI (PetL)
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Q9M3L0
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: F, N
Length: 131 amino acids
Theoretical weight: 12.95 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: PetM family of cytochrome b6f complex subunit 7
Length: 131 amino acids
Theoretical weight: 12.95 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
A0A9R0IV89 (Residues: 1-131; Coverage: 100%)
Pfam: PetM family of cytochrome b6f complex subunit 7
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A0A9R0IV89
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: G, O
Length: 37 amino acids
Theoretical weight: 4.17 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: Cytochrome B6-F complex subunit 5
Length: 37 amino acids
Theoretical weight: 4.17 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P69461 (Residues: 1-37; Coverage: 100%)
Pfam: Cytochrome B6-F complex subunit 5
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P69461
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: H, P
Length: 29 amino acids
Theoretical weight: 3.17 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: PetN
Length: 29 amino acids
Theoretical weight: 3.17 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P61045 (Residues: 1-29; Coverage: 100%)
Pfam: PetN
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P61045
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: Q, R
Length: 103 amino acids
Theoretical weight: 10.61 KDa
Source organism: Spinacia oleracea
UniProt:
Pfam: Thylakoid soluble phosphoprotein TSP9
Length: 103 amino acids
Theoretical weight: 10.61 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
Q8GT36 (Residues: 1-103; Coverage: 100%)
Pfam: Thylakoid soluble phosphoprotein TSP9
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Q8GT36
Chains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces
Sequence conservation