6YNU: CaM-P458 complex

CaM-P458 complex (crystal form 1). Determined by X-ray diffraction at 3.12 Å resolution. Released 17 Mar 2021.

Method: X-ray diffraction
Resolution: 3.12 Å
Organisms: Homo sapiens, Bordetella pertussis
Chains: 4
Atoms: 2,665
Mol. weight: 38.81 kDa
Ligands: CA
Released: 17 Mar 2021

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

Secondary structure: helices and β-sheets

6YNU contains 16 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: 7 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	27	1	1
α-helix	29-38	10
α-helix	45-55	11
β-strand	63	1	1
α-helix	65-92	28
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

Chains B and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	460-480	21

Chain C: 7 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	27	1	3
α-helix	29-38	10
α-helix	45-55	11
β-strand	63	1	3
α-helix	65-92	28
β-strand	99-100	2	4
α-helix	102-112	11
α-helix	118-128	11
β-strand	136-137	2	4
α-helix	138-145	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin-1	A, C	protein	148	Homo sapiens	P0DP23 (AlphaFold model)
Bifunctional adenylate cyclase toxin/hemolysin CyaA	B, D	protein	24	Bordetella pertussis	P0DKX7 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6YNU_1 Calmodulin-1 (chains A, C)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK

Sequence of entity 2 (B, D), FASTA

>6YNU_2 Bifunctional adenylate cyclase toxin/hemolysin CyaA (chains B, D)
WGQRALQGAQAVAAAQRLVHAIAL

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	9

Primary citation

A High-Affinity Calmodulin-Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells. Voegele, A., Sadi, M., O'Brien, D.P. et al. Adv Sci (Weinh) (2021) 8:2003630-2003630. DOI 10.1002/advs.202003630 · 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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