6KN7: Actin, alpha skeletal muscle

Structure of human cardiac thin filament in the calcium free state. Determined by electron microscopy at 6.6 Å resolution. Released 15 Jan 2020.

Method: Electron microscopy
Resolution: 6.6 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 29
Atoms: 61,916
Mol. weight: 896.58 kDa
Ligands: ADP
Released: 15 Jan 2020

Explore 6KN7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6KN7 contains 434 α-helices and 348 β-strands across 29 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	88-148	61
α-helix	200-215	16
α-helix	226-270	45

Chain A: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	22	1	2
β-strand	24	1	2
β-strand	29-32	4	1
β-strand	35-38	4	3
β-strand	53-54	2	3
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	3
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-86	8
α-helix	87-93	7
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-145	9
β-strand	150-153	4	5
β-strand	160	1	6
β-strand	163-166	4	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	178	1	6
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-230	8
α-helix	234-236	3
β-strand	238-241	4	7
β-strand	247-250	4	7
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-299	3	5
α-helix	309-320	12
α-helix	322	1
β-strand	329-330	2	5
α-helix	338-347	10
α-helix	350-352	3
α-helix	356	1
β-strand	357-358	2	1
α-helix	361-365	5
α-helix	367-369	3
α-helix	370-373	4

Chain b: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	43-79	37
α-helix	81-83	3
α-helix	90-140	51
α-helix	141-143	3
α-helix	150-153	4
α-helix	157-183	27

Chain B: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	8
β-strand	16-21	6	8
β-strand	22	1	9
β-strand	24	1	9
β-strand	29-32	4	8
β-strand	35-38	4	10
β-strand	53-54	2	10
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	10
β-strand	71-72	2	11
β-strand	75-76	2	11
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	8
α-helix	113-125	13
β-strand	131-136	6	8
α-helix	137-143	7
β-strand	150-155	6	12
β-strand	160	1	12
β-strand	163-166	4	12
β-strand	169-170	2	12
α-helix	172-174	3
β-strand	178	1	12
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-230	8
α-helix	234-236	3
β-strand	238-241	4	13
β-strand	247-250	4	13
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-301	5	12
α-helix	309-318	10
α-helix	322	1
α-helix	326-327	2
β-strand	329-330	2	12
α-helix	338-348	11
α-helix	350-352	3
α-helix	356	1
β-strand	357-358	2	8
α-helix	361-365	5
α-helix	367-369	3
α-helix	370-373	4

Chain c: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-10	6
α-helix	14-24	11
α-helix	25-27	3
β-strand	37	1	20
α-helix	38-40	3
α-helix	41-47	7
α-helix	54-62	9
β-strand	71	1	20
α-helix	74-81	8
α-helix	94-104	11
β-strand	111-112	2	21
α-helix	114-122	9
α-helix	130-140	11
β-strand	148-149	2	21
α-helix	150-156	7

Chain C: 24 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	14
β-strand	16-21	6	14
β-strand	29-32	4	14
β-strand	35-38	4	15
β-strand	42	1	5
β-strand	53-54	2	15
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	15
β-strand	71-72	2	16
β-strand	75-76	2	16
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	14
α-helix	113-125	13
β-strand	131-136	6	14
α-helix	137-145	9
β-strand	150-154	5	17
β-strand	160	1	18
β-strand	163-166	4	17
β-strand	169-170	2	17
α-helix	172-174	3
β-strand	178	1	18
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-230	8
α-helix	234-236	3
β-strand	238-241	4	19
β-strand	247-250	4	19
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	17
α-helix	309-318	10
α-helix	322	1
β-strand	329-330	2	17
α-helix	338-347	10
α-helix	350-352	3
α-helix	356	1
β-strand	357-358	2	14
α-helix	361-365	5
α-helix	367-369	3
α-helix	370-373	4

Chain D: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	22
β-strand	16-21	6	22
β-strand	29-32	4	22
β-strand	35-38	4	23
β-strand	42	1	12
β-strand	53-54	2	23
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	23
β-strand	71-72	2	24
β-strand	75-76	2	24
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	22
α-helix	114-125	12
β-strand	131-136	6	22
α-helix	137-145	9
β-strand	150-153	4	25
β-strand	160	1	26
β-strand	163-166	4	25
β-strand	169-170	2	25
α-helix	172-174	3
β-strand	178	1	26
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-230	8
α-helix	234-236	3
β-strand	238-241	4	27
β-strand	247-250	4	27
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-299	3	25
α-helix	309-318	10
α-helix	322	1
β-strand	329-330	2	25
α-helix	338-348	11
α-helix	350-355	6
α-helix	356	1
β-strand	357-358	2	22
α-helix	361-365	5
α-helix	367-369	3
α-helix	370-373	4

Chain E: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	28
β-strand	16-21	6	28
β-strand	29-32	4	28
β-strand	35-38	4	29
β-strand	42	1	17
β-strand	53-54	2	29
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	29
β-strand	71-72	2	30
β-strand	75-76	2	30
α-helix	79-86	8
α-helix	87-93	7
α-helix	98-100	3
β-strand	103-107	5	28
α-helix	113-125	13
β-strand	131-136	6	28
α-helix	137-145	9
β-strand	150-153	4	31
β-strand	160	1	32
β-strand	163-166	4	31
β-strand	169-170	2	31
α-helix	172-174	3
β-strand	178	1	32
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-230	8
α-helix	234-236	3
β-strand	238-241	4	33
β-strand	247-250	4	33
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-293	7
β-strand	297-299	3	31
α-helix	309-320	12
α-helix	322	1
β-strand	329-330	2	31
α-helix	338-347	10
α-helix	350-354	5
α-helix	356	1
β-strand	357-358	2	28
α-helix	361-365	5
α-helix	367-369	3
α-helix	370-373	4

17 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, alpha skeletal muscle	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
Tropomyosin alpha-1 chain	P, Q, W, X	protein	274	Homo sapiens	P09493 (AlphaFold model)
Tropomyosin alpha-1 chain	R, S, Y, Z	protein	31	Homo sapiens	P09493 (AlphaFold model)
Troponin T, cardiac muscle	T, a	protein	186	Homo sapiens	P45379 (AlphaFold model)
Troponin I, cardiac muscle	U, b	protein	170	Homo sapiens	P19429 (AlphaFold model)
Troponin C, slow skeletal and cardiac muscles	V, c	protein	160	Homo sapiens	P63316

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

>6KN7_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (P, Q, W, X), FASTA

>6KN7_2 Tropomyosin alpha-1 chain (chains P, Q, W, X)
LKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEK
LELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI
ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKC
AELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLE
KSIDDLEDELYAQKLKYKAISEELDHALNDMTSI

Sequence of entity 3 (R, S, Y, Z), FASTA

>6KN7_3 Tropomyosin alpha-1 chain (chains R, S, Y, Z)
ASMDAIKKKMQMLKLDKENALDRAEQAEADK

Sequence of entity 4 (T, a), FASTA

>6KN7_4 Troponin T, cardiac muscle (chains T, a)
FDDIHRKRMEKDLNELQALIEAHFENRKKEEEELVSLKDRIERRRAERAEQQRIRNEREK
ERQNRLAEERARREEEENRRKAEDEARKKKALSNMMHFGGYIQKQAQTERKSGKRQTERE
KKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNLEAEKFDLQEKFKQQKYEINVLRN
RINDNQ

Sequence of entity 5 (U, b), FASTA

>6KN7_5 Troponin I, cardiac muscle (chains U, b)
ISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQL
HARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLG
ARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES

Sequence of entity 6 (V, c), FASTA

>6KN7_6 Troponin C, slow skeletal and cardiac muscles (chains V, c)
DDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMI
DEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIML
QATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	15

Primary citation

Cardiac muscle thin filament structures reveal calcium regulatory mechanism. Yamada, Y., Namba, K., Fujii, T. Nat Commun (2020) 11:153-153. DOI 10.1038/s41467-019-14008-1 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
1WUA 1.45 Å, The structure of Aplyronine A-actin complex
2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
1J6Z 1.54 Å, Uncomplexed actin
1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A

Browse structure collections

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