5U6Y: Pseudo-atomic model of the CaMKIIa holoenzyme

Pseudo-atomic model of the CaMKIIa holoenzyme. Determined by electron microscopy at 20.0 Å resolution. Released 21 Jun 2017.

Method: Electron microscopy
Resolution: 20.0 Å
Organism: Rattus norvegicus
Chains: 12
Atoms: 43,896
Mol. weight: 627.38 kDa
Released: 21 Jun 2017

Explore 5U6Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5U6Y contains 289 α-helices and 228 β-strands across 12 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: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	1
β-strand	25-32	8	1
β-strand	37-45	9	1
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	2
α-helix	73-74	2
β-strand	75-80	6	1
β-strand	84-89	6	1
β-strand	95-96	2	2
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	3
α-helix	138-140	3
β-strand	141-143	3	2
α-helix	150-151	2
β-strand	152-154	3	2
β-strand	161-162	2	3
β-strand	169	1	4
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	4
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-299	16
α-helix	310-313	4
α-helix	327-328	2
α-helix	336	1
α-helix	345-362	18
α-helix	366-371	6
β-strand	373-380	8	5
α-helix	382-384	3
β-strand	388-390	3	5
α-helix	393-400	8
β-strand	411-421	11	5
β-strand	426-438	13	5
β-strand	444-457	14	5
β-strand	462-470	9	5

Chain B: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	6
β-strand	25-32	8	6
β-strand	37-45	9	6
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	7
α-helix	73-74	2
β-strand	75-80	6	6
β-strand	84-89	6	6
β-strand	95-96	2	7
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	8
α-helix	138-140	3
β-strand	141-143	3	7
α-helix	150-151	2
β-strand	152-154	3	7
β-strand	161-162	2	8
β-strand	169	1	9
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	9
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-299	16
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	10
α-helix	382-384	3
β-strand	388-390	3	10
α-helix	393-400	8
β-strand	411-421	11	10
β-strand	426-438	13	10
β-strand	444-457	14	10
β-strand	462-470	9	10

Chain C: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	11
β-strand	25-32	8	11
β-strand	37-45	9	11
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	12
α-helix	73-74	2
β-strand	75-80	6	11
β-strand	84-89	6	11
β-strand	95-96	2	12
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	13
α-helix	138-140	3
β-strand	141-143	3	12
α-helix	150-151	2
β-strand	152-154	3	12
β-strand	161-162	2	13
β-strand	169	1	14
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	14
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	256-258	3
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-298	15
α-helix	308-311	4
α-helix	334-338	5
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	15
α-helix	382-384	3
β-strand	388-390	3	15
α-helix	393-400	8
β-strand	411-421	11	15
β-strand	426-438	13	15
β-strand	444-457	14	15
β-strand	462-470	9	15

Chains D and F: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	16
β-strand	25-32	8	16
β-strand	37-45	9	16
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	17
α-helix	73-74	2
β-strand	75-80	6	16
β-strand	84-89	6	16
β-strand	95-96	2	17
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	18
α-helix	138-140	3
β-strand	141-143	3	17
α-helix	150-151	2
β-strand	152-154	3	17
β-strand	161-162	2	18
β-strand	169	1	19
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	19
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	256-258	3
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-299	16
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	20
α-helix	382-384	3
β-strand	388-390	3	20
α-helix	393-400	8
β-strand	411-421	11	20
β-strand	426-438	13	20
β-strand	444-457	14	20
β-strand	462-470	9	20

Chain E: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	21
β-strand	25-32	8	21
β-strand	37-45	9	21
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	22
α-helix	73-74	2
β-strand	75-80	6	21
β-strand	84-89	6	21
β-strand	95-96	2	22
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	23
α-helix	138-140	3
β-strand	141-143	3	22
α-helix	150-151	2
β-strand	152-154	3	22
β-strand	161-162	2	23
β-strand	169	1	24
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	24
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	256-258	3
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-299	16
α-helix	336-339	4
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	25
α-helix	382-384	3
β-strand	388-390	3	25
α-helix	393-400	8
β-strand	411-421	11	25
β-strand	426-438	13	25
β-strand	444-457	14	25
β-strand	462-470	9	25

Chain G: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	31
β-strand	25-32	8	31
β-strand	37-45	9	31
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	32
α-helix	73-74	2
β-strand	75-80	6	31
β-strand	84-89	6	31
β-strand	95-96	2	32
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	33
α-helix	138-140	3
β-strand	141-143	3	32
α-helix	150-151	2
β-strand	152-154	3	32
β-strand	161-162	2	33
β-strand	169	1	34
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	34
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	256-258	3
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-299	16
α-helix	311-313	3
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	35
α-helix	382-384	3
β-strand	388-390	3	35
α-helix	393-400	8
β-strand	411-421	11	35
β-strand	426-438	13	35
β-strand	444-457	14	35
β-strand	462-470	9	35

Chain H: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	36
β-strand	25-32	8	36
β-strand	37-45	9	36
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	37
α-helix	73-74	2
β-strand	75-80	6	36
β-strand	84-89	6	36
β-strand	95-96	2	37
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	38
α-helix	138-140	3
β-strand	141-143	3	37
α-helix	150-151	2
β-strand	152-154	3	37
β-strand	161-162	2	38
β-strand	169	1	39
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	39
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	256-258	3
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-300	17
α-helix	312-314	3
α-helix	326-328	3
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	40
α-helix	382-384	3
β-strand	388-390	3	40
α-helix	393-400	8
β-strand	411-421	11	40
β-strand	426-438	13	40
β-strand	444-457	14	40
β-strand	462-470	9	40

Chain I: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	13-21	9	41
β-strand	25-32	8	41
β-strand	37-45	9	41
α-helix	46-48	3
α-helix	51-55	5
α-helix	57-66	10
β-strand	72	1	42
α-helix	73-74	2
β-strand	75-80	6	41
β-strand	84-89	6	41
β-strand	95-96	2	42
α-helix	97-102	6
α-helix	109-128	20
β-strand	131-132	2	43
α-helix	138-140	3
β-strand	141-143	3	42
α-helix	150-151	2
β-strand	152-154	3	42
β-strand	161-162	2	43
β-strand	169	1	44
α-helix	177-179	3
α-helix	182-186	5
β-strand	190	1	44
α-helix	193-208	16
α-helix	218-227	10
α-helix	242-251	10
α-helix	256-258	3
α-helix	260-261	2
α-helix	262-266	5
α-helix	269-272	4
α-helix	274-277	4
α-helix	284-299	16
α-helix	306-308	3
α-helix	346-362	17
α-helix	366-371	6
β-strand	373-380	8	45
α-helix	382-384	3
β-strand	388-390	3	45
α-helix	393-400	8
β-strand	411-421	11	45
β-strand	426-438	13	45
β-strand	444-457	14	45
β-strand	462-470	9	45

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium/calmodulin-dependent protein kinase type II subunit alpha	A, B, C, D, E, F, G, H, I, J, K, L	protein	461	Rattus norvegicus	P11275 (AlphaFold model)

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

>5U6Y_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha (chains A, B, C, D, E, F, G, H, I, J, K, L)
MYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPN
IVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGV
VHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYG
KPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKM
LTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATR
NFSGGKSGGNKKSDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTK
MCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAY
IRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGA

Primary citation

The CaMKII holoenzyme structure in activation-competent conformations. Myers, J.B., Zaegel, V., Coultrap, S.J. et al. Nat Commun (2017) 8:15742-15742. DOI 10.1038/ncomms15742 · PubMed

Other PDB entries of the same protein (UniProt P11275 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CDM 2.0 Å, Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray…
1CM1 2.0 Å, Motions of calmodulin-single-conformer refinement
1CM4 2.0 Å, Motions of calmodulin-four-conformer refinement
8SYG 2.6 Å, Cryo-EM structure of tetradecameric hub domain of CaMKII alpha
8T15 2.7 Å, Cryo-EM structure of dodecameric hub domain of CaMKII alpha

Browse structure collections

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