4OVN: Calmodulin

Voltage-gated Sodium Channel 1.5 (Nav1.5) C-terminal domain in complex with Calmodulin poised for activation. Determined by X-ray diffraction at 2.8 Å resolution. Released 3 Dec 2014.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 10
Atoms: 11,784
Mol. weight: 180.93 kDa
Ligands: MG, PO4
Released: 3 Dec 2014

Explore 4OVN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4OVN contains 79 α-helices and 41 β-strands across 10 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: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	9-20	12
β-strand	27-29	3	1
α-helix	30-38	9
α-helix	46-56	11
β-strand	63-65	3	1
α-helix	66-78	13
α-helix	80-81	2
α-helix	84-91	8
β-strand	100-101	2	2
α-helix	103-112	10
α-helix	116-118	3
α-helix	119-129	11
β-strand	137-138	2	2
α-helix	139-143	5

Chain B: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-20	11
β-strand	27-29	3	4
α-helix	30-33	4
α-helix	34-39	6
α-helix	46-50	5
β-strand	63-65	3	4
α-helix	66-69	4
α-helix	73-76	4
α-helix	83-93	11
β-strand	101-102	2	5
α-helix	103-112	10
α-helix	119-129	11
β-strand	136-137	2	5
α-helix	139-144	6

Chain C: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	9-20	12
β-strand	27-29	3	7
α-helix	33-38	6
α-helix	48-56	9
β-strand	63-65	3	7
α-helix	66-78	13
α-helix	83-91	9
β-strand	100-102	3	8
α-helix	103-112	10
α-helix	116-118	3
α-helix	119-129	11
β-strand	136-138	3	8
α-helix	139-145	7

Chain D: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	9-20	12
β-strand	27-29	3	11
α-helix	32-39	8
α-helix	46-56	11
β-strand	63-65	3	11
α-helix	66-78	13
α-helix	82-91	10
β-strand	100-102	3	12
α-helix	103-112	10
α-helix	119-129	11
β-strand	136-138	3	12
α-helix	139-144	6

Chain E: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-19	10
β-strand	27-28	2	14
α-helix	31-38	8
α-helix	48-50	3
β-strand	64-65	2	14
α-helix	66-75	10
α-helix	84-92	9
β-strand	100-101	2	15
α-helix	103-110	8
α-helix	116-118	3
α-helix	119-129	11
β-strand	137-138	2	15
α-helix	139-145	7

Chain F: 6 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	1791-1801	11
β-strand	1808-1810	3	3
α-helix	1814-1819	6
α-helix	1832-1837	6
β-strand	1841-1843	3	3
β-strand	1847-1849	3	3
α-helix	1850-1862	13
α-helix	1868-1881	14
β-strand	1891-1894	4	3
α-helix	1897-1924	28

Chain G: 7 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	1788-1801	14
β-strand	1808-1810	3	6
α-helix	1811-1813	3
α-helix	1814-1820	7
α-helix	1832-1836	5
β-strand	1841-1843	3	6
β-strand	1847-1849	3	6
α-helix	1850-1862	13
α-helix	1868-1882	15
β-strand	1891-1894	4	6
α-helix	1896-1925	30

Chain H: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	1788-1801	14
β-strand	1808-1810	3	9
α-helix	1814-1820	7
α-helix	1832-1838	7
β-strand	1841-1842	2	10
β-strand	1843	1	9
β-strand	1847-1849	3	9
α-helix	1850-1862	13
α-helix	1868-1882	15
β-strand	1893-1894	2	10
α-helix	1895-1923	29

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin	A, B, C, D, E	protein	149	Homo sapiens	P0DP23 (AlphaFold model)
Sodium channel protein type 5 subunit alpha	F, G, H, I, J	protein	157	Homo sapiens	Q14524 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>4OVN_1 Calmodulin (chains A, B, C, D, E)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Sequence of entity 2 (F, G, H, I, J), FASTA

>4OVN_2 Sodium channel protein type 5 subunit alpha (chains F, G, H, I, J)
ENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQ
ISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPI
TTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFR

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	18
PO4	Phosphate ion	O4 P	2

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

Primary citation

Regulation of the NaV1.5 cytoplasmic domain by calmodulin. Gabelli, S.B., Boto, A., Kuhns, V.H. et al. Nat Commun (2014) 5:5126. DOI 10.1038/ncomms6126 · 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

Browse structure collections

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