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Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of calmodulin kinase I

Solution NMR
PDB entry 2l7l coloured by chain, front view.
PDB entry 2l7l coloured by chain, side view.
PDB entry 2l7l coloured by chain, top view.
Source organisms:
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Calmodulin-1 and Calcium/calmodulin-dependent protein kinase type 1
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Multimeric state: hetero dimer
Accessible surface area: 8785.32 Å2
Buried surface area: 3051.24 Å2
Dissociation area: 1,481.09 Å2
Dissociation energy (ΔGdiss): 19.6 kcal/mol
Dissociation entropy (TΔSdiss): 9.38 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-143953

Macromolecules

Calmodulin-1
Chain: A
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 2-149; Coverage: 99%)
Gene names: CALM, CALM1, CAM, CAM1
Pfam: EF-hand domain pair
InterPro:
Calmodulin-1 in PDB entry 2l7l, assembly 1, front view.
Calmodulin-1 in PDB entry 2l7l, assembly 1, side view.
Calmodulin-1 in PDB entry 2l7l, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P0DP23  
114820406080100120140
 
50100
UniProt
P0DP23
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
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Calcium/calmodulin-dependent protein kinase type 1
Chain: B
Length: 22 amino acids
Theoretical weight: 2.61 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q63450 (Residues: 299-320; Coverage: 6%)
Gene name: Camk1
Calcium/calmodulin-dependent protein kinase type 1 in PDB entry 2l7l, assembly 1, front view.
Calcium/calmodulin-dependent protein kinase type 1 in PDB entry 2l7l, assembly 1, side view.
Calcium/calmodulin-dependent protein kinase type 1 in PDB entry 2l7l, assembly 1, top view.
PDBe-KB: UniProt Coverage View: Q63450  
122246810121416182022
 
1020AKSKWKQAFNATAVVRHMRKLQ
UniProt
Q63450
Chains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Molecule details ›

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