› 7bf2

X-ray diffraction
1.43Å resolution

Ca2+-Calmodulin in complex with human muscle form creatine kinase peptide in extended 1:2 binding mode

Released:
DOI: 10.2210/pdb7bf2/pdb
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PDB entry 7bf2 coloured by chain, front view.
PDB entry 7bf2 coloured by chain, side view.
PDB entry 7bf2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Calmodulin complexes with brain and muscle creatine kinase peptides.
Sprenger J, Trifan A, Patel N, Vanderbeck A, Bredfelt J, Tajkhorshid E, Rowlett R, Lo Leggio L, Åkerfeldt KS, Linse S
OpenAccess logo Curr Res Struct Biol 3 121-132 (2021)
PMID: 34235492

Function and Biology Details

Reaction catalysed: 
ATP + creatine = ADP + phosphocreatine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139187 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chain: AAA
Molecule details ›
Chain: AAA
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 1-149; Coverage: 100%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Creatine kinase M-type Chains: CCC, DDD
Molecule details ›
Chains: CCC, DDD
Length: 18 amino acids
Theoretical weight: 2.25 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P06732 (Residues: 301-318; Coverage: 5%)
Gene names: CKM, CKMM

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: C2
Unit cell:
a: 105.695Å b: 24.53Å c: 60.349Å
α: 90° β: 104.838° γ: 90°
R-values:
R R work R free
0.202 0.201 0.228
Expression systems:
  • Escherichia coli
  • Not provided

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Citations

1 review citation

Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin.
Bej et al. (2022)

2 mentions without citation

NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel.
Bej et al. (2022)
1 more

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