Solution NMR structure of CaM bound to iNOS CaM binding domain peptide. Determined by solution NMR. Released 16 May 2012.
Explore 2LL6 in 3D Show helices and sheets RCSB PDB PDBe
2LL6 contains 9 α-helices and 4 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 | 6-19 | 14 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 29-37 | 9 | |
| α-helix | 45-55 | 11 | |
| β-strand | 62-63 | 2 | 1 |
| α-helix | 65-75 | 11 | |
| α-helix | 82-92 | 11 | |
| β-strand | 99-100 | 2 | 2 |
| α-helix | 102-110 | 9 | |
| α-helix | 118-128 | 11 | |
| β-strand | 136-137 | 2 | 2 |
| α-helix | 138-143 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 152-163 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 148 | Homo sapiens | P0DP23 (AlphaFold model) |
| Nitric oxide synthase, inducible | B | protein | 17 | Homo sapiens | P35228 (AlphaFold model) |
>2LL6_1 Calmodulin (chains A) ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEEFVQMMTAK
>2LL6_2 Nitric oxide synthase, inducible (chains B) LKVLVKAVLFACMLMRK
Structure and Dynamics of Calmodulin (CaM) Bound to Nitric Oxide Synthase Peptides: Effects of a Phosphomimetic CaM Mutation. Piazza, M., Futrega, K., Spratt, D.E. et al. Biochemistry (2012) 51:3651-3661. DOI 10.1021/bi300327z · PubMed
Other PDB entries of the same protein (UniProt P0DP23 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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