6U3A: Calmodulin-1

1.65 Angstrom crystal structure of the N97S Ca-CaM:CaV1.2 IQ domain complex. Determined by X-ray diffraction at 1.65 Å resolution. Released 19 Feb 2020.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,044
Mol. weight: 42.35 kDa
Ligands: CA
Released: 19 Feb 2020

Explore 6U3A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6U3A contains 18 α-helices and 8 β-strands across 4 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

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	1
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	1
α-helix	65-78	14
α-helix	81-92	12
β-strand	99-101	3	2
α-helix	102-112	11
α-helix	118-128	11
β-strand	135-137	3	2
α-helix	138-146	9

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	3
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	3
α-helix	65-77	13
α-helix	82-92	11
β-strand	99-100	2	4
α-helix	102-111	10
α-helix	118-128	11
β-strand	136-137	2	4
α-helix	138-145	8

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1613-1636	24

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1618-1636	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin-1	A, B	protein	148	Homo sapiens	P0DP23 (AlphaFold model)
Voltage-dependent L-type calcium channel subunit alpha-1C	C, D	protein	37	Homo sapiens	Q13936 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6U3A_1 Calmodulin-1 (chains A, B)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGSGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK

Sequence of entity 2 (C, D), FASTA

>6U3A_2 Voltage-dependent L-type calcium channel subunit alpha-1C (chains C, D)
SNADEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPS

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	7

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

Primary citation

Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+binding and cause misfolding. Wang, K., Brohus, M., Holt, C. et al. J Physiol (2020) 598:1169-1186. DOI 10.1113/JP279307 · 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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