Calmodulin and Nm peptide complex. Determined by X-ray diffraction at 2.69 Å resolution. Released 20 Mar 2013.
Explore 4E53 in 3D Show helices and sheets RCSB PDB PDBe
4E53 contains 19 α-helices and 8 β-strands across 2 chains. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-20 | 11 | |
| β-strand | 28 | 1 | 1 |
| α-helix | 30-39 | 10 | |
| α-helix | 50-56 | 7 | |
| β-strand | 64 | 1 | 1 |
| α-helix | 66-93 | 28 | |
| β-strand | 101-102 | 2 | 2 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-127 | 9 | |
| β-strand | 136-137 | 2 | 2 |
| α-helix | 139-146 | 8 | |
| α-helix | 156-172 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| β-strand | 28 | 1 | 3 |
| α-helix | 31-37 | 7 | |
| α-helix | 38-40 | 3 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64 | 1 | 3 |
| α-helix | 66-86 | 21 | |
| β-strand | 100-102 | 3 | 4 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 4 |
| α-helix | 139-145 | 7 | |
| α-helix | 159-161 | 3 | |
| α-helix | 162-165 | 4 | |
| α-helix | 167-170 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin, Linker, IQ motif of Neuromodulin | A, B | protein | 185 | Mus musculus | P06837 (AlphaFold model), P0DP26 (AlphaFold model) |
>4E53_1 Calmodulin, Linker, IQ motif of Neuromodulin (chains A, B) MHHHHHHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI NEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNL GEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAKGGGGGAATKIQASFRGHITRKKLK GEKKG
Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin. Kumar, V., Chichili, V.P.R., Zhong, L. et al. Sci Rep (2013) 3:1392-1392. DOI 10.1038/srep01392 · PubMed
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