7LZ4: PDB entry 7LZ4

Crystal structure of A211D mutant of Protein Kinase A RIa subunit, a Carney Complex mutation. Determined by X-ray diffraction at 4.16 Å resolution. Released 26 May 2021.

Method: X-ray diffraction
Resolution: 4.16 Å
Organism: Bos taurus
Chains: 8
Atoms: 17,138
Mol. weight: 248.02 kDa
Ligands: CMP
Released: 26 May 2021

Explore 7LZ4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LZ4 contains 98 α-helices and 119 β-strands across 8 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: 11 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	120-131	12
α-helix	134-137	4
α-helix	141-150	10
β-strand	152-156	5	1
β-strand	161-163	3	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	201-204	4
β-strand	212-215	4	2
β-strand	219-225	7	1
α-helix	226-244	19
α-helix	253-255	3
α-helix	259-268	10
β-strand	270-274	5	3
β-strand	279-281	3	3
β-strand	289-302	14	3
β-strand	311-316	6	3
β-strand	321-322	2	3
α-helix	324-328	5
β-strand	336-349	14	3
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-366	6

Chain B: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	120-132	13
α-helix	134-137	4
α-helix	141-150	10
β-strand	152-156	5	4
β-strand	161-163	3	5
β-strand	171-177	7	4
β-strand	180-184	5	5
β-strand	187-192	6	5
β-strand	197-198	2	4
α-helix	201-204	4
α-helix	207-209	3
β-strand	212-215	4	5
β-strand	219-225	7	4
α-helix	226-249	24
α-helix	254-256	3
α-helix	259-268	10
β-strand	270-274	5	6
β-strand	278-281	4	6
β-strand	289-301	13	6
β-strand	315-316	2	6
β-strand	321-322	2	6
α-helix	324-329	6
β-strand	336-349	14	6
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-366	6

Chain C: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	114	1	7
α-helix	120-131	12
α-helix	134-137	4
α-helix	141-150	10
β-strand	152-156	5	8
β-strand	161-163	3	9
β-strand	171-177	7	8
β-strand	180-184	5	9
β-strand	187-192	6	9
β-strand	197-198	2	8
α-helix	201-204	4
β-strand	212-215	4	9
β-strand	219-225	7	8
α-helix	226-249	24
α-helix	253-256	4
α-helix	259-268	10
α-helix	269	1
β-strand	270-272	3	10
β-strand	276	1	10
β-strand	278-281	4	10
β-strand	283	1	11
β-strand	289-299	11	10
β-strand	315-316	2	10
β-strand	321-322	2	10
α-helix	324-329	6
β-strand	333	1	11
β-strand	337-349	13	10
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-366	6

Chain D: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	120-132	13
α-helix	134-137	4
α-helix	141-150	10
β-strand	152-156	5	12
β-strand	161-163	3	13
β-strand	171-177	7	12
β-strand	180-184	5	13
β-strand	187-192	6	13
β-strand	197-198	2	12
α-helix	201-204	4
α-helix	207-209	3
β-strand	212-215	4	13
β-strand	219-225	7	12
α-helix	226-232	7
α-helix	234-245	12
α-helix	246-248	3
α-helix	253-255	3
α-helix	259-268	10
β-strand	271-274	4	14
β-strand	279-281	3	14
β-strand	289-302	14	14
β-strand	311-316	6	14
β-strand	321-322	2	14
α-helix	326-329	4
β-strand	336-349	14	14
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-366	6

Chain E: 11 helices, 14 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	15
β-strand	161-163	3	16
β-strand	171-177	7	15
β-strand	179-184	6	16
β-strand	187-193	7	16
β-strand	197-198	2	15
α-helix	201-204	4
β-strand	212-215	4	16
β-strand	219-225	7	15
α-helix	226-249	24
α-helix	253-255	3
α-helix	259-268	10
β-strand	270-274	5	17
β-strand	279-281	3	17
β-strand	289-301	13	17
β-strand	314-316	3	17
β-strand	321-322	2	17
α-helix	324-328	5
β-strand	336-349	14	17
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-369	9

Chain F: 12 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	111	1	7
α-helix	120-131	12
α-helix	134-136	3
α-helix	141-150	10
β-strand	152-156	5	18
β-strand	161-163	3	19
β-strand	171-177	7	18
β-strand	179-184	6	19
β-strand	187-193	7	19
β-strand	197-198	2	18
α-helix	201-204	4
β-strand	212-215	4	19
β-strand	219-225	7	18
α-helix	226-232	7
α-helix	234-244	11
α-helix	246-248	3
α-helix	253-255	3
α-helix	259-268	10
β-strand	270-274	5	20
β-strand	279-281	3	20
β-strand	286	1	21
β-strand	289-301	13	20
β-strand	314-316	3	20
β-strand	321-322	2	20
α-helix	324-328	5
β-strand	332	1	21
β-strand	336-349	14	20
α-helix	350-356	7
α-helix	361-366	6

Chain G: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	120-132	13
α-helix	135-137	3
α-helix	141-150	10
β-strand	152-156	5	22
β-strand	161-163	3	23
β-strand	171-177	7	22
β-strand	180-184	5	23
β-strand	187-192	6	23
β-strand	197-198	2	22
α-helix	201-204	4
α-helix	207-209	3
β-strand	212-215	4	23
β-strand	219-225	7	22
α-helix	226-249	24
α-helix	253-255	3
α-helix	259-268	10
β-strand	270-274	5	24
β-strand	279-281	3	24
β-strand	289-302	14	24
β-strand	311-316	6	24
β-strand	321-322	2	24
α-helix	324-328	5
β-strand	336-349	14	24
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-366	6

Chain H: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	120-131	12
α-helix	134-137	4
α-helix	141-150	10
β-strand	152-156	5	25
β-strand	161-163	3	26
β-strand	171-177	7	25
β-strand	180-184	5	26
β-strand	187-192	6	26
β-strand	197-198	2	25
α-helix	201-204	4
α-helix	207-209	3
β-strand	212-215	4	26
β-strand	219-225	7	25
α-helix	226-232	7
α-helix	234-244	11
α-helix	246-248	3
α-helix	253-256	4
α-helix	259-268	10
β-strand	271-272	2	27
β-strand	278-281	4	27
β-strand	289-299	11	27
β-strand	315-316	2	27
β-strand	321-322	2	27
α-helix	324-328	5
β-strand	337-349	13	27
α-helix	350-356	7
α-helix	358-360	3
α-helix	361-369	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed	A, B, C, D, E, F, G, H	protein	269	Bos taurus	P00514 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>7LZ4_1 cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed (chains A, B, C, D, E, F, G, H)
AASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGD
EGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRADTVKAKTNVKLWGIDRD
SYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPG
DEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVK
LDRPRFERVLGPCSDILKRNIQQYNSFVS

Ligands and cofactors

ID	Name	Formula	Copies
CMP	Adenosine-3',5'-cyclic-monophosphate	C10 H12 N5 O6 P	16

Primary citation

Noncanonical protein kinase A activation by oligomerization of regulatory subunits as revealed by inherited Carney complex mutations. Jafari, N., Del Rio, J., Akimoto, M. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2024716118 · PubMed

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

3PNA 1.5 Å, Crystal Structure of cAMP bound (91-244)RIa Subunit of cAMP-dependent Protein Kinase
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

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