1CDL: Calmodulin

Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Aug 1994.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 5,287
Mol. weight: 76.15 kDa
Ligands: CA
Released: 31 Aug 1994

Explore 1CDL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CDL contains 36 α-helices and 16 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, 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	65-73	9
α-helix	78-92	15
β-strand	99-100	2	2
α-helix	102-111	10
α-helix	118-128	11
β-strand	136-137	2	2
α-helix	138-145	8

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	3
α-helix	29-37	9
α-helix	45-55	11
β-strand	63-64	2	3
α-helix	65-72	8
α-helix	78-92	15
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: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	5
α-helix	29-38	10
α-helix	45-53	9
β-strand	63-64	2	5
α-helix	65-73	9
α-helix	78-92	15
β-strand	99-100	2	6
α-helix	102-112	11
α-helix	118-128	11
β-strand	136-137	2	6
α-helix	138-144	7

Chain D: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	7
α-helix	29-38	10
α-helix	45-53	9
β-strand	63-64	2	7
α-helix	65-73	9
α-helix	78-92	15
β-strand	99-100	2	8
α-helix	102-112	11
α-helix	118-126	9
β-strand	136-137	2	8
α-helix	138-144	7

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	798-813	16

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	798-812	15

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	797-812	16

Chain H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	799-814	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin	A, B, C, D	protein	147	Homo sapiens	P0DP23 (AlphaFold model)
Calcium/calmodulin-dependent protein kinase type II alpha chain	E, F, G, H	protein	20		P11799 (AlphaFold model)

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

>1CDL_1 CALMODULIN (chains A, B, C, D)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTA

Sequence of entity 2 (E, F, G, H), FASTA

>1CDL_2 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II ALPHA CHAIN (chains E, F, G, H)
ARRKWQKTGHAVRAIGRLSS

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	16

Primary citation

Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Meador, W.E., Means, A.R., Quiocho, F.A. Science (1992) 257:1251-1255. 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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