2LL6: CaM

Solution NMR structure of CaM bound to iNOS CaM binding domain peptide. Determined by solution NMR. Released 16 May 2012.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,301
Mol. weight
18.69 kDa
Released
16 May 2012

Explore 2LL6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 8 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix6-1914
β-strand27-2821
α-helix29-379
α-helix45-5511
β-strand62-6321
α-helix65-7511
α-helix82-9211
β-strand99-10022
α-helix102-1109
α-helix118-12811
β-strand136-13722
α-helix138-1436
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix152-16312

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein148Homo sapiensP0DP23 (AlphaFold model)
Nitric oxide synthase, inducibleBprotein17Homo sapiensP35228 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LL6_1 Calmodulin (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Sequence of entity 2 (B), FASTA
>2LL6_2 Nitric oxide synthase, inducible (chains B)
LKVLVKAVLFACMLMRK

Primary citation

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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