3B32: Calmodulin

Crystal Structure of Calcium-Saturated Calmodulin N-Terminal Domain Fragment, Residues 1-75. Determined by X-ray diffraction at 1.6 Å resolution. Released 13 Nov 2007.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Rattus norvegicus
Chains
1
Atoms
683
Mol. weight
8.4 kDa
Ligands
CA
Released
13 Nov 2007

Explore 3B32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3B32 contains 4 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix6-1914
β-strand2711
α-helix29-3810
α-helix45-539
β-strand6311
α-helix65-739

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein75Rattus norvegicusP0DP29 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3B32_1 Calmodulin (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2

Primary citation

Thermodynamics and conformational change governing domain-domain interactions of calmodulin. O'Donnell, S.E., Newman, R.A., Witt, T.J. et al. Methods Enzymol (2009) 466:503-526. DOI 10.1016/S0076-6879(09)66021-3 · PubMed

Other PDB entries of the same protein (UniProt P0DP29 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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