Structure analysis

Crystal structure of apoCaM bound to the gating domain of small conductance Ca2+-activated potassium channel

X-ray diffraction
3.09Å resolution
Source organism: Rattus norvegicus
Assemblies composition:
homo dimer
hetero dimer (preferred)
homo trimer
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 3 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 9000 Å2
Buried surface area: 800 Å2
Dissociation area: 400 Å2
Dissociation energy (ΔGdiss): -1 kcal/mol
Dissociation entropy (TΔSdiss): 7 kcal/mol
Interface energy (ΔGint): -4 kcal/mol
Symmetry number: 1
Assembly 4
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Multimeric state: homo trimer
Accessible surface area: 18600 Å2
Buried surface area: 9000 Å2
Dissociation area: 2,000 Å2
Dissociation energy (ΔGdiss): 4 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -46 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B, I, M, R
Length: 148 amino acids
Theoretical weight: 17.14 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DP29 (Residues: 2-149; Coverage: 99%)
Gene names: CaMI, Calm, Calm1, Cam, Cam1
Pfam: EF-hand domain pair
InterPro:
CATH: EF-hand
SCOP: Calmodulin-like

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Chain: D
Length: 85 amino acids
Theoretical weight: 10.22 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P70604 (Residues: 411-489; Coverage: 14%)
Gene name: Kcnn2
Pfam: Calmodulin binding domain
InterPro:

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