6CXJ: Actin, cytoplasmic 2

Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2. Determined by electron microscopy at 11.0 Å resolution. Released 10 Oct 2018.

Method: Electron microscopy
Resolution: 11.0 Å
Organism: Homo sapiens
Chains: 20
Atoms: 25,305
Mol. weight: 379.11 kDa
Released: 10 Oct 2018

Explore 6CXJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CXJ contains 137 α-helices and 198 β-strands across 20 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: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
β-strand	15-20	6	1
β-strand	28-31	4	1
β-strand	34-37	4	2
β-strand	52-53	2	2
α-helix	55-59	5
β-strand	64-67	4	2
β-strand	70-71	2	3
β-strand	74-75	2	3
α-helix	78-86	9
α-helix	87-92	6
β-strand	102-106	5	1
α-helix	112-124	13
β-strand	130-135	6	1
α-helix	136-144	9
β-strand	149-153	5	4
β-strand	159-165	7	4
β-strand	168-169	2	4
α-helix	171-173	3
β-strand	175-177	3	4
α-helix	181-195	15
α-helix	202-214	13
α-helix	222-228	7
α-helix	229-231	3
β-strand	237-240	4	5
α-helix	241	1
β-strand	246-249	4	5
α-helix	251-261	11
α-helix	263-265	3
α-helix	273-283	11
α-helix	286-294	9
β-strand	296-299	4	4
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	4
α-helix	334-336	3
α-helix	337-347	11
α-helix	349-354	6
β-strand	356-357	2	1
α-helix	358-364	7
α-helix	368-372	5

Chain B: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	6
β-strand	15-20	6	6
β-strand	28-31	4	6
β-strand	34-37	4	7
α-helix	40-41	2
β-strand	52-53	2	7
α-helix	55-59	5
β-strand	64-67	4	7
β-strand	70-71	2	8
β-strand	74-75	2	8
α-helix	78-87	10
α-helix	88-92	5
β-strand	102-106	5	6
α-helix	112-125	14
β-strand	130-135	6	6
α-helix	136-144	9
β-strand	149-154	6	9
β-strand	159-165	7	9
β-strand	168-169	2	9
α-helix	171-173	3
β-strand	175-177	3	9
α-helix	181-194	14
α-helix	202-214	13
α-helix	222-227	6
α-helix	228-231	4
β-strand	237-240	4	10
α-helix	241	1
β-strand	246-249	4	10
α-helix	251-261	11
α-helix	263-265	3
α-helix	273-283	11
α-helix	286-293	8
β-strand	296-297	2	11
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	11
α-helix	337-345	9
α-helix	349-354	6
β-strand	356-357	2	6
α-helix	358-364	7
α-helix	368-372	5

Chain C: 19 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	12
β-strand	15-20	6	12
β-strand	28-31	4	12
β-strand	34-37	4	13
β-strand	52-53	2	13
α-helix	55-59	5
β-strand	64-67	4	13
β-strand	70-71	2	14
β-strand	74-75	2	14
α-helix	78-86	9
α-helix	87-92	6
β-strand	102-106	5	12
α-helix	112-124	13
β-strand	130-135	6	12
α-helix	136-144	9
β-strand	149-154	6	15
β-strand	159-165	7	15
β-strand	168-169	2	15
α-helix	171-173	3
β-strand	175-177	3	15
α-helix	181-195	15
α-helix	202-214	13
α-helix	222-228	7
β-strand	237-240	4	16
β-strand	246-249	4	16
α-helix	252-261	10
α-helix	263-265	3
α-helix	273-283	11
α-helix	286-294	9
β-strand	296-299	4	15
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	15
α-helix	337-347	11
α-helix	349-354	6
β-strand	356-357	2	12
α-helix	358-364	7
α-helix	368-372	5

Chain D: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	7-12	6	17
β-strand	15-20	6	17
β-strand	28-31	4	17
β-strand	34-37	4	18
α-helix	40-41	2
β-strand	52-53	2	18
α-helix	55-59	5
β-strand	64-67	4	18
β-strand	70-71	2	19
β-strand	74-75	2	19
α-helix	78-86	9
α-helix	87-92	6
β-strand	102-106	5	17
α-helix	112-124	13
β-strand	130-135	6	17
α-helix	136-144	9
β-strand	149-154	6	20
β-strand	159-165	7	20
β-strand	168-169	2	20
α-helix	171-173	3
β-strand	175-177	3	20
α-helix	181-195	15
α-helix	202-214	13
α-helix	222-228	7
α-helix	229-231	3
β-strand	237-240	4	21
β-strand	246-249	4	21
α-helix	251-261	11
α-helix	263-265	3
α-helix	273-283	11
α-helix	286-294	9
β-strand	296-299	4	20
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	20
α-helix	337-347	11
α-helix	349-354	6
β-strand	356-357	2	17
α-helix	358-363	6
α-helix	368-372	5

Chain E: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	22
β-strand	15-20	6	22
β-strand	28-31	4	22
β-strand	34-37	4	23
α-helix	40-41	2
β-strand	52-53	2	23
α-helix	55-59	5
β-strand	64-67	4	23
β-strand	70-71	2	24
β-strand	74-75	2	24
α-helix	78-87	10
α-helix	88-92	5
β-strand	102-106	5	22
α-helix	112-124	13
β-strand	130-135	6	22
α-helix	136-144	9
β-strand	149-154	6	25
β-strand	159-165	7	25
β-strand	168-169	2	25
β-strand	175-177	3	25
α-helix	181-195	15
α-helix	202-214	13
α-helix	222-228	7
α-helix	229-231	3
β-strand	237-240	4	26
α-helix	241	1
β-strand	246-249	4	26
α-helix	252-261	10
α-helix	273-283	11
α-helix	286-294	9
β-strand	296-300	5	25
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	25
α-helix	337-345	9
α-helix	349-354	6
β-strand	356-357	2	22
α-helix	358-364	7
α-helix	368-372	5

Chain G: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	152-154	3
β-strand	157-159	3	27
β-strand	164-167	4	28
β-strand	172-179	8	27
β-strand	188-193	6	28
β-strand	197-198	2	28
α-helix	199-202	4
β-strand	207-214	8	27
β-strand	219-226	8	27
α-helix	231-233	3
β-strand	235-242	8	28
β-strand	247-257	11	28

Chain H: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	157-159	3	29
β-strand	164-167	4	30
β-strand	172-179	8	29
α-helix	186-187	2
β-strand	188-193	6	30
β-strand	197-198	2	30
α-helix	199-202	4
β-strand	207-214	8	29
β-strand	219-226	8	29
α-helix	231-233	3
β-strand	235-242	8	30
β-strand	247-257	11	30

Chain I: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	152-154	3
β-strand	157-159	3	31
β-strand	164-166	3	32
β-strand	172-179	8	31
β-strand	188-193	6	32
β-strand	197-198	2	32
α-helix	199-202	4
β-strand	207-214	8	31
β-strand	219-226	8	31
α-helix	231-233	3
β-strand	235-242	8	32
β-strand	247-256	10	32

11 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
Actin, cytoplasmic 2	A, B, C, D, E	protein	375	Homo sapiens	P63261 (AlphaFold model)
Myosin-binding protein C, cardiac-type	G, H, I, J, K, L	protein	109	Homo sapiens	Q14896 (AlphaFold model)
Myosin-binding protein C, cardiac-type	M, N, O, P, Q	protein	101	Homo sapiens	Q14896 (AlphaFold model)
Tropomyosin	S, T, U, V	protein	127	Homo sapiens

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

>6CXJ_1 Actin, cytoplasmic 2 (chains A, B, C, D, E)
MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Sequence of entity 2 (G, H, I, J, K, L), FASTA

>6CXJ_2 Myosin-binding protein C, cardiac-type (chains G, H, I, J, K, L)
MDDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQL
HDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHE

Sequence of entity 3 (M, N, O, P, Q), FASTA

>6CXJ_3 Myosin-binding protein C, cardiac-type (chains M, N, O, P, Q)
MPEPGKKPVSAFSKKPRSVEVAAGSPAVFEAETERAGVKVRWQRGGSDISASNKYGLATE
GTRHTLTVREVGPADQGSYAVIAGSSKVKFDLKVIEAEKAE

Sequence of entity 4 (S, T, U, V), FASTA

>6CXJ_4 Tropomyosin (chains S, T, U, V)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXX

Primary citation

N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament. Risi, C., Belknap, B., Forgacs-Lonart, E. et al. Structure (2018) 26:1604. DOI 10.1016/j.str.2018.08.007 · PubMed

Other PDB entries of the same protein (UniProt P63261 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6WK2 1.76 Å, SETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with Methionine
6WK1 1.89 Å, SETD3 in Complex with an Actin Peptide with His73 Replaced with Methionine
6V63 2.02 Å, SETD3 WT in Complex with an Actin Peptide with His73 Replaced with Glutamine
6V62 2.36 Å, SETD3 double mutant (N255F/W273A) in Complex with an Actin Peptide with His73 Replaced…
7NVM 3.1 Å, Human TRiC complex in closed state with nanobody Nb18, actin and PhLP2A bound
8DNF 3.38 Å, Cryo-EM structure of nonmuscle gamma-actin
9SMX 3.67 Å, CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules
5JLH 3.9 Å, Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution
6G2T 9.0 Å, human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament
6CXI 11.0 Å, Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C…

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