2QCS: PDB entry 2QCS

A complex structure between the Catalytic and Regulatory subunit of Protein Kinase A that represents the inhibited state. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Nov 2007.

Method
X-ray diffraction
Resolution
2.2 Å
Organisms
Mus musculus, Bos taurus
Chains
2
Atoms
5,459
Mol. weight
75.15 kDa
Ligands
MN, ANP, TAM
Released
6 Nov 2007

Explore 2QCS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2QCS contains 31 α-helices and 31 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: 17 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix14-3118
α-helix40-423
β-strand43-5191
β-strand56-6271
β-strand68-7581
α-helix76-816
α-helix85-9713
β-strand10312
α-helix104-1052
β-strand106-11161
β-strand115-12171
α-helix1221
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-helix219-23315
α-helix243-25210
α-helix263-27210
α-helix289-2924
α-helix295-2973
α-helix302-3065
Chain B: 14 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix94-974
β-strand98-9925
α-helix105-1095
α-helix120-12910
α-helix134-1374
α-helix141-15010
β-strand152-15656
β-strand161-16337
β-strand16818
α-helix1691
β-strand171-17776
β-strand180-18457
β-strand187-19267
β-strand197-19826
α-helix200-2034
β-strand20818
β-strand212-21547
β-strand219-22576
α-helix226-24924
α-helix252-2543
α-helix259-26810
β-strand270-27459
β-strand279-28139
β-strand289-303159
β-strand310-31679
β-strand321-32229
α-helix325-3273
β-strand336-349149
α-helix350-3578
α-helix360-3645
α-helix368-3747

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase, alpha-catalytic subunitAprotein350Mus musculusP05132 (AlphaFold model)
cAMP-dependent protein kinase type I-alpha regulatory subunitBprotein291Bos taurusP00514 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2QCS_1 cAMP-dependent protein kinase, alpha-catalytic subunit (chains A)
GNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLV
KHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM
EYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI
QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA
DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT
DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
Sequence of entity 2 (B), FASTA
>2QCS_2 cAMP-dependent protein kinase type I-alpha regulatory subunit (chains B)
KGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFD
AMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPR
AATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADAL
EPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLM
NRPKAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSVA

Ligands and cofactors

IDNameFormulaCopies
MNManganese (II) ionMn2
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31
TAMTris(hydroxyethyl)aminomethaneC7 H17 N O31

Water and common crystallization additives (SO4, ACT, GOL) are not listed.

Primary citation

PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation. Kim, C., Cheng, C.Y., Saldanha, S.A. et al. Cell (2007) 130:1032-1043. DOI 10.1016/j.cell.2007.07.018 · 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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