5DOW: Calmodulin

Solution of the Variably-Twinned Structure of a Novel Calmodulin-Peptide Complex in a Novel Configuration. Determined by X-ray diffraction at 1.7 Å resolution. Released 10 Aug 2016.

Method: X-ray diffraction
Resolution: 1.7 Å
Organisms: Homo sapiens, Mus musculus
Chains: 8
Atoms: 6,881
Mol. weight: 78.65 kDa
Ligands: CA
Released: 10 Aug 2016

Explore 5DOW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5DOW contains 41 α-helices and 18 β-strands across 8 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, 5 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	27-28	2	1
α-helix	30-39	10
β-strand	42	1	2
α-helix	46-56	11
β-strand	64-65	2	1
α-helix	66-76	11
α-helix	83-93	11
β-strand	100-101	2	3
α-helix	103-112	10
α-helix	119-129	11
β-strand	137-138	2	3
α-helix	139-147	9

Chains B, F and H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	566-576	11
α-helix	579-582	4

Chain C: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	28	1	4
α-helix	30-39	10
β-strand	42	1	2
α-helix	46-54	9
β-strand	64	1	4
α-helix	66-79	14
α-helix	82-93	12
β-strand	100-101	2	5
α-helix	103-112	10
α-helix	119-129	11
β-strand	137-138	2	5
α-helix	139-146	8

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	564-566	3
α-helix	567-576	10
α-helix	579-582	4

Chain E: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	28	1	6
α-helix	30-39	10
α-helix	46-54	9
β-strand	64	1	6
α-helix	66-79	14
α-helix	82-93	12
β-strand	100-101	2	7
α-helix	103-112	10
α-helix	119-129	11
β-strand	137-138	2	7
α-helix	139-146	8

Chain G: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	28	1	8
α-helix	30-39	10
α-helix	46-54	9
β-strand	64	1	8
α-helix	66-78	13
α-helix	82-93	12
β-strand	101	1	9
α-helix	103-112	10
α-helix	119-129	11
β-strand	137	1	9
α-helix	139-146	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin	A, C, E, G	protein	148	Homo sapiens	P0DP23 (AlphaFold model)
Chloride anion exchanger	B, D, F, H	protein	22	Mus musculus	Q9WVC8 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>5DOW_1 Calmodulin (chains A, C, E, G)
AYQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK

Sequence of entity 2 (B, D, F, H), FASTA

>5DOW_2 Chloride anion exchanger (chains B, D, F, H)
KRNKALKKIRKLQKRGLIQMTX

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	16

Water and common crystallization additives (NA, CL, SO4) are not listed.

Primary citation

Solution of the structure of a calmodulin-peptide complex in a novel configuration from a variably twinned data set. Keller, J.P. Acta Crystallogr D Struct Biol (2017) 73:22-31. DOI 10.1107/S2059798316019318 · PubMed

Other PDB entries of the same protein (UniProt P0DP23 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9MXD 1.17 Å, Human E104A calmodulin:MLCK RM20 complex
7BF1 1.24 Å, Ca2+-Calmodulin in complex with peptide from brain-type creatine kinase in extended 1:2…
6XXX 1.25 Å, 1.25 Angstrom crystal structure of Ca/CaM A102V:RyR2 peptide complex
4DJC 1.35 Å, 1.35 A crystal structure of the NaV1.5 DIII-IV-Ca/CaM complex
7BF2 1.43 Å, Ca2+-Calmodulin in complex with human muscle form creatine kinase peptide in extended…
2F3Y 1.45 Å, Calmodulin/IQ domain complex
2W73 1.45 Å, High-resolution structure of the complex between calmodulin and a peptide from…
4LZX 1.5 Å, Complex of IQCG and Ca2+-free CaM
5V03 1.58 Å, A positive allosteric modulator binding pocket in SK2 ion channels is shared by Riluzole…
9MVW 1.58 Å, Crystal structure of S101F calmodulin - CaM:RM20 analog complex
2F3Z 1.6 Å, Calmodulin/IQ-AA domain complex
6M7H 1.6 Å, Structure of calmodulin with KN93

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