3PNA: PDB entry 3PNA

Crystal Structure of cAMP bound (91-244)RIa Subunit of cAMP-dependent Protein Kinase. Determined by X-ray diffraction at 1.5 Å resolution. Released 9 Feb 2011.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Bos taurus
Chains: 2
Atoms: 2,490
Mol. weight: 35.43 kDa
Ligands: CMP
Released: 9 Feb 2011

Explore 3PNA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PNA contains 16 α-helices and 16 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: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	120-132	13
α-helix	134-136	3
α-helix	141-150	10
β-strand	152-156	5	1
β-strand	161-163	3	2
α-helix	168-169	2
β-strand	171-177	7	1
β-strand	180-184	5	2
β-strand	187-192	6	2
β-strand	197-198	2	1
α-helix	201-205	5
α-helix	207-209	3
β-strand	212-215	4	2
β-strand	219-225	7	1
α-helix	226-228	3
α-helix	229-233	5
α-helix	234-239	6

Chain B: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	120-132	13
α-helix	134-136	3
α-helix	141-150	10
β-strand	152-156	5	3
β-strand	161-163	3	4
α-helix	168-169	2
β-strand	171-177	7	3
β-strand	180-184	5	4
β-strand	187-192	6	4
β-strand	197-198	2	3
α-helix	200-205	6
α-helix	207-209	3
β-strand	212-215	4	4
β-strand	219-225	7	3
α-helix	226-233	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cAMP-dependent protein kinase type I-alpha regulatory subunit	A, B	protein	154	Bos taurus	P00514 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3PNA_1 cAMP-dependent protein kinase type I-alpha regulatory subunit (chains A, B)
GRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDA
MFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRA
ATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMY

Ligands and cofactors

ID	Name	Formula	Copies
CMP	Adenosine-3',5'-cyclic-monophosphate	C10 H12 N5 O6 P	2

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

Primary citation

Cyclic AMP Analog Blocks Kinase Activation by Stabilizing Inactive Conformation: Conformational Selection Highlights a New Concept in Allosteric Inhibitor Design. Badireddy, S., Yunfeng, G., Ritchie, M. et al. Mol Cell Proteomics (2011) 10:M110.004390-M110.004390. DOI 10.1074/mcp.M110.004390 · PubMed

Other PDB entries of the same protein (UniProt P00514 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FHI 2.0 Å, Crystal structure of a complex between the catalytic and regulatory (RI{alpha}) subunits…
3IM3 2.0 Å, Crystal structure of PKA RI alpha dimerization/docking domain
5HVZ 2.0 Å, Crystal structure of smAKAP AKB domain bound RIa dimerization/docking (D/D) complex at…
2QCS 2.2 Å, A complex structure between the Catalytic and Regulatory subunit of Protein Kinase A…
3IM4 2.29 Å, Crystal structure of cAMP-dependent Protein Kinase A Regulatory Subunit I alpha in…
1NE6 2.3 Å, Crystal structure of Sp-cAMP binding R1a subunit of cAMP-dependent protein kinase
3PLQ 2.3 Å, Crystal structure of PKA type I regulatory subunit bound with Rp-8-Br-cAMPS
1NE4 2.4 Å, Crystal Structure of Rp-cAMP Binding R1a Subunit of cAMP-dependent Protein Kinase
4X6R 2.4 Å, An Isoform-specific Myristylation Switch Targets RIIb PKA Holoenzymes to Membranes
1RL3 2.7 Å, Crystal structure of cAMP-free R1a subunit of PKA
3IIA 2.7 Å, Crystal structure of apo (91-244) RIa subunit of cAMP-dependent protein kinase
1RGS 2.8 Å, Regulatory subunit of camp dependent protein kinase

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