8UKO: CAMP-dependent protein kinase A catalytic domain

cAMP-dependent protein kinase A catalytic domain in complex with voltage gated calcium channel peptide ternary complex 2. Determined by X-ray diffraction at 2.89 Å resolution. Released 11 Dec 2024.

Method
X-ray diffraction
Resolution
2.89 Å
Organisms
Mus musculus, Homo sapiens
Chains
2
Atoms
2,821
Mol. weight
42.09 kDa
Ligands
ANP, MG
Released
11 Dec 2024

Explore 8UKO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8UKO contains 22 α-helices and 15 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 C: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand1982-198325
Chain E: 22 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix16-3116
α-helix40-423
β-strand43-5191
β-strand55-6281
β-strand68-7581
α-helix76-816
α-helix85-9713
β-strand10312
α-helix104-1052
β-strand106-11271
β-strand115-12061
α-helix121-1233
β-strand12712
α-helix128-1358
α-helix140-15920
β-strand162-16323
α-helix169-1713
β-strand172-17432
β-strand180-18232
β-strand189-19023
β-strand19514
β-strand199-20025
α-helix202-2043
α-helix207-2104
β-strand21514
α-helix218-23316
α-helix243-25210
α-helix256-2583
α-helix263-27210
α-helix277-2793
α-helix289-2924
α-helix295-2973
α-helix302-3065
α-helix311-3122
α-helix334-3363
α-helix345-3495

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase catalytic subunit alphaEprotein339Mus musculusP05132 (AlphaFold model)
Arg-gly-phe-leu-arg-ser-ala-ser-leu-gly-arg-arg-ala-ser-phe-his-leuCprotein17Homo sapiensQ13936 (AlphaFold model)
Sequence of entity 1 (E), FASTA
>8UKO_1 cAMP-dependent protein kinase catalytic subunit alpha (chains E)
SNAVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAM
KILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSH
LRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRV
KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV
SGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVE
APFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
Sequence of entity 2 (C), FASTA
>8UKO_2 ARG-GLY-PHE-LEU-ARG-SER-ALA-SER-LEU-GLY-ARG-ARG-ALA-SER-PHE-HIS-LEU (chains C)
RGFLRSASLGRRASFHL

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31
MGMagnesium ionMg2

Primary citation

Crystallographic, kinetic, and calorimetric investigation of PKA interactions with L-type calcium channels and Rad GTPase. Yoo, R., Haji-Ghassemi, O., Bader, M. et al. J Biol Chem (2024) 301:108039-108039. DOI 10.1016/j.jbc.2024.108039 · PubMed

Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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