9PC1: PDB entry 9PC1

Co-crystal structure of the cAMP-dependent protein kinase catalytic subunit alpha with the inhibitor BLU0588. Determined by X-ray diffraction at 1.55 Å resolution. Released 13 May 2026.

Method: X-ray diffraction
Resolution: 1.55 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 3,304
Mol. weight: 43.31 kDa
Ligands: A1CHQ
Released: 13 May 2026

Explore 9PC1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PC1 contains 21 α-helices and 13 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 E: 19 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	13-30	18
α-helix	33-34	2
α-helix	40-42	3
β-strand	43-51	9	1
β-strand	55-62	8	1
β-strand	68-75	8	1
α-helix	76-81	6
α-helix	85-97	13
β-strand	103	1	2
α-helix	104-105	2
β-strand	106-111	6	1
β-strand	115-121	7	1
β-strand	127	1	2
α-helix	128-135	8
α-helix	140-159	20
β-strand	162-163	2	3
α-helix	169-171	3
β-strand	172-174	3	2
β-strand	180-182	3	2
β-strand	189-190	2	3
β-strand	195	1	4
α-helix	202-204	3
α-helix	207-210	4
β-strand	215	1	4
α-helix	218-233	16
α-helix	243-251	9
α-helix	263-272	10
α-helix	289-292	4
α-helix	295-297	3
α-helix	302-306	5
α-helix	311-312	2
α-helix	345-347	3

Chain I: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	6-12	7
α-helix	18-22	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cAMP-dependent protein kinase catalytic subunit alpha	E	protein	350	Mus musculus	P05132 (AlphaFold model)
cAMP-dependent protein kinase inhibitor alpha	I	protein	19	Homo sapiens	P61925 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>9PC1_1 cAMP-dependent protein kinase catalytic subunit alpha (chains E)
GNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLV
KHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM
EYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI
QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA
DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT
DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF

Sequence of entity 2 (I), FASTA

>9PC1_2 cAMP-dependent protein kinase inhibitor alpha (chains I)
TTYADFIASGRTGRRNAIH

Ligands and cofactors

ID	Name	Formula	Copies
A1CHQ	(6M)-N-[(1R,2R)-2-(pyrrolidin-1-yl)-2,3-dihydro-1H-inden-1-yl]-6-(1H-pyrrolo[2,…	C26 H25 N5 O	1

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

Primary citation

A PKA-selective inhibitor captures an open but more ordered conformation of the PKA catalytic subunit. Bruystens, J.G.H., Wu, J., Tan, G. et al. Proc Natl Acad Sci U S A (2026) 123:e2536312123-e2536312123. DOI 10.1073/pnas.2536312123 · PubMed

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

1RDQ 1.26 Å, Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase
4DFX 1.35 Å, Crystal structure of myristoylated K7C catalytic subunit of cAMP-dependent protein…
4HPU 1.55 Å, Crystal structure of the catalytic subunit of cAMP-dependent protein kinase displaying…
4IAI 1.55 Å, X-ray Structure of cAMP dependent protein kinase A in complex with high Ca2+…
3FJQ 1.6 Å, Crystal structure of cAMP-dependent protein kinase catalytic subunit alpha in complex…
4IAK 1.6 Å, Low temperature X-ray structure of cAMP dependent protein kinase A in complex with high…
3IDB 1.62 Å, Crystal structure of (108-268)RIIb:C holoenzyme of cAMP-dependent protein kinase
4IB1 1.63 Å, Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP…
7V0G 1.63 Å, Structure of cAMP-dependent protein kinase using a MD-MX procedure, produced using 1.63…
3QAL 1.7 Å, Crystal Structure of Arg280Ala mutant of Catalytic subunit of cAMP-dependent Protein…
3X2W 1.7 Å, Michaelis complex of cAMP-dependent Protein Kinase Catalytic Subunit
4O22 1.7 Å, Binary complex of metal-free PKAc with SP20.

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