1CDK: Camp-dependent protein kinase

Camp-dependent protein kinase catalytic subunit (E.C.2.7.1.37) (protein kinase A) complexed with protein kinase inhibitor peptide fragment 5-24 (PKI(5-24) isoelectric variant ca) and MN2+ adenylyl imidodiphosphate (mnamp-pnp) at PH 5.6 and 7C and 4C. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Oct 1995.

Method
X-ray diffraction
Resolution
2.0 Å
Organisms
Sus scrofa, Homo sapiens
Chains
4
Atoms
6,361
Mol. weight
87.39 kDa
Ligands
MYR, ANP, MN
Released
15 Oct 1995

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

Secondary structure: helices and β-sheets

1CDK contains 40 α-helices and 26 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: 19 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix10-3122
α-helix40-423
β-strand43-5191
β-strand56-6271
β-strand68-7581
α-helix76-816
α-helix85-9713
β-strand10312
β-strand106-11161
β-strand115-12061
α-helix121-1222
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
α-helix202-2043
α-helix207-2104
β-strand21514
α-helix219-23315
α-helix243-25210
α-helix263-27210
α-helix289-2924
α-helix295-2973
α-helix302-3065
α-helix311-3122
α-helix331-3344
α-helix345-3473
Chain B: 17 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix9-3123
α-helix40-423
β-strand43-5195
β-strand56-6275
β-strand68-7585
α-helix76-816
α-helix85-9713
β-strand10316
β-strand106-11165
β-strand115-12065
β-strand12716
α-helix128-1358
α-helix140-15920
β-strand162-16327
α-helix169-1713
β-strand172-17436
β-strand180-18236
β-strand189-19027
β-strand19518
α-helix202-2043
α-helix207-2115
β-strand21518
α-helix218-23316
α-helix243-25210
α-helix256-2583
α-helix263-27210
α-helix289-2924
α-helix295-2973
α-helix302-3065
α-helix315-3173
Chain I: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-76
α-helix16-183
Chain J: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-87
α-helix14-185

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Camp-dependent protein kinaseA, Bprotein350Sus scrofaP36887 (AlphaFold model)
Protein kinase inhibitorI, Jprotein20Homo sapiensP61926 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1CDK_1 CAMP-DEPENDENT PROTEIN KINASE (chains A, B)
GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV
KHKETGNHFAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVM
EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI
QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA
DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKDGVNDIKNHKWFATT
DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Sequence of entity 2 (I, J), FASTA
>1CDK_2 PROTEIN KINASE INHIBITOR (chains I, J)
TTYADFIASGRTGRRNAIHD

Ligands and cofactors

IDNameFormulaCopies
MYRMyristic acidC14 H28 O22
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32
MNManganese (II) ionMn4

Primary citation

Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). Bossemeyer, D., Engh, R.A., Kinzel, V. et al. EMBO J (1993) 12:849-859. PubMed

Other PDB entries of the same protein (UniProt P36887 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1CDK directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.