1VRK: Calmodulin

The 1.9 Å structure of E84K-calmodulin RS20 peptide complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 27 Apr 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: synthetic construct
Chains: 2
Atoms: 1,492
Mol. weight: 19.19 kDa
Ligands: CA
Released: 27 Apr 1999

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

Secondary structure: helices and β-sheets

1VRK 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

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	100	1	2
α-helix	102-111	10
α-helix	118-128	11
β-strand	136	1	2
α-helix	138-145	8

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin	A	protein	148	synthetic construct
RS20	B	protein	21		P11799 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1VRK_1 CALMODULIN (chains A)
ADQLTDEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLNLMARKMKDTDSEEKLKEAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEE
VDEMIREADVDGDGQVNYEEFVQVMMAK

Sequence of entity 2 (B), FASTA

>1VRK_2 RS20 (chains B)
RRKWQKTGHAVRAIGRLSSSX

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	4

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

Primary citation

Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties. Mirzoeva, S., Weigand, S., Lukas, T.J. et al. Biochemistry (1999) 38:3936-3947. DOI 10.1021/bi9821263 · PubMed

Other PDB entries of the same protein (UniProt P11799 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2O5G 1.08 Å, Calmodulin-smooth muscle light chain kinase peptide complex
1QTX 1.65 Å, The 1.65 Å structure of calmodulin RS20 peptide complex
1QS7 1.8 Å, The 1.8 angstrom structure of calmodulin rs20 peptide complex
9U9D 1.8 Å, Bipartite Genetically Encoded Biosensor sG-GECO1
1CDL 2.0 Å, Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
3EVR 2.0 Å, Crystal structure of Calcium bound monomeric GCAMP2
4OY4 2.03 Å, calcium-free CaMPARI v0.2
2K0F Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light…

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