8ZB7: Human left ventricle ATM complex

Human left ventricle ATM complex. Determined by electron microscopy at 3.19 Å resolution. Released 29 Jan 2025.

Method: Electron microscopy
Resolution: 3.19 Å
Organism: Homo sapiens
Chains: 16
Atoms: 58,698
Mol. weight: 857.09 kDa
Ligands: ADP
Released: 29 Jan 2025

Explore 8ZB7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8ZB7 contains 364 α-helices and 324 β-strands across 16 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.

Chains A and E: 23 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	97
β-strand	11	1	98
β-strand	17-19	3	98
β-strand	21	1	97
β-strand	29-31	3	98
β-strand	35-38	4	99
β-strand	53-54	2	99
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	99
β-strand	71	1	100
β-strand	76	1	100
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	97
α-helix	113-125	13
β-strand	131-136	6	97
α-helix	137-145	9
β-strand	150-155	6	101
β-strand	160-166	7	101
β-strand	169-170	2	101
α-helix	172-174	3
β-strand	176-178	3	101
α-helix	182-192	11
α-helix	193-196	4
α-helix	205-216	12
α-helix	223-232	10
β-strand	238-242	5	102
β-strand	245-250	6	102
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	101
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	101
α-helix	338-348	11
α-helix	350-354	5
β-strand	357-358	2	97
α-helix	359-365	7
α-helix	367-370	4

Chain B: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-9	2	12
β-strand	11	1	13
β-strand	17-19	3	13
β-strand	21	1	12
β-strand	29-31	3	13
β-strand	35-38	4	14
β-strand	53-54	2	14
α-helix	57-60	4
α-helix	62-64	3
β-strand	65-68	4	14
β-strand	71	1	15
β-strand	76	1	15
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	12
α-helix	113-125	13
β-strand	131-136	6	12
α-helix	137-144	8
β-strand	150-155	6	16
β-strand	160-166	7	16
β-strand	169-170	2	16
α-helix	172-174	3
β-strand	176-178	3	16
α-helix	182-193	12
α-helix	194-196	3
α-helix	205-216	12
α-helix	223-232	10
β-strand	238-243	6	17
β-strand	245-250	6	17
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	16
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	16
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	12
α-helix	359-365	7
α-helix	367-369	3

Chain C: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	18
β-strand	11	1	19
β-strand	17-19	3	19
β-strand	21	1	18
β-strand	29-31	3	19
β-strand	35-38	4	20
β-strand	53-54	2	20
α-helix	57-59	3
β-strand	65-68	4	20
β-strand	71	1	21
β-strand	76	1	21
α-helix	80-88	9
α-helix	89-94	6
β-strand	103-107	5	18
α-helix	113-125	13
β-strand	131-136	6	18
α-helix	137-145	9
β-strand	150-155	6	22
β-strand	160-166	7	22
β-strand	169-170	2	22
α-helix	172-174	3
β-strand	176-178	3	22
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-242	5	23
β-strand	245-250	6	23
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	22
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	22
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	18
α-helix	359-365	7
α-helix	367-370	4

Chain D: 21 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	24
β-strand	11	1	25
β-strand	17-19	3	25
β-strand	21	1	24
β-strand	29-31	3	25
β-strand	35-38	4	26
β-strand	53-54	2	26
α-helix	57-60	4
β-strand	65-68	4	26
β-strand	71	1	27
β-strand	76	1	27
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	24
α-helix	113-125	13
β-strand	131-136	6	24
α-helix	137-144	8
β-strand	150-154	5	28
β-strand	160-166	7	28
β-strand	169-170	2	28
α-helix	172-174	3
β-strand	176-178	3	28
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-240	3	29
β-strand	248-250	3	29
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	28
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	28
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	24
α-helix	359-365	7
α-helix	367-370	4

Chain F: 21 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	36
β-strand	11	1	37
β-strand	17-19	3	37
β-strand	21	1	36
β-strand	29-31	3	37
β-strand	35-38	4	38
β-strand	53-54	2	38
α-helix	57-60	4
α-helix	61-64	4
β-strand	65-68	4	38
β-strand	71	1	39
β-strand	76	1	39
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	36
α-helix	113-125	13
β-strand	131-136	6	36
α-helix	137-144	8
β-strand	150-155	6	40
β-strand	160-166	7	40
β-strand	169-170	2	40
α-helix	172-174	3
β-strand	176-178	3	40
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-243	6	41
β-strand	245-250	6	41
α-helix	253-256	4
α-helix	258-261	4
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	40
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	40
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	36
α-helix	359-365	7
α-helix	366-371	6

Chains G, H, I, J, K and M: 38 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	13-16	4
α-helix	20-27	8
β-strand	38	1	42
β-strand	39-40	2	43
β-strand	46-47	2	43
β-strand	49-51	3	44
β-strand	55	1	45
β-strand	58	1	45
β-strand	61-63	3	44
β-strand	68-69	2	44
β-strand	77	1	42
α-helix	78-81	4
α-helix	82-84	3
β-strand	89	1	46
α-helix	90-92	3
α-helix	98-110	13
β-strand	115-117	3	46
β-strand	122-125	4	46
α-helix	126-127	2
α-helix	132-134	3
α-helix	136-142	7
α-helix	151-152	2
α-helix	154-168	15
β-strand	172-177	6	46
α-helix	184-198	15
α-helix	217-230	14
β-strand	232-233	2	47
β-strand	241-242	2	47
β-strand	247-252	6	46
β-strand	258-264	7	46
α-helix	271-273	3
β-strand	283	1	47
α-helix	284-290	7
α-helix	295-301	7
α-helix	307-309	3
α-helix	311-314	4
α-helix	325-337	13
α-helix	343-359	17
β-strand	364-366	3	48
β-strand	373-375	3	48
α-helix	379-388	10
α-helix	392-400	9
β-strand	403-406	4	49
β-strand	409-412	4	49
α-helix	413-414	2
α-helix	417-447	31
β-strand	454-461	8	46
β-strand	471	1	50
α-helix	473-504	32
α-helix	515-521	7
α-helix	530-539	10
α-helix	545-556	12
β-strand	564	1	50
β-strand	577-581	5	50
β-strand	584-588	5	50
α-helix	593-597	5
β-strand	598	1	51
α-helix	603-610	8
α-helix	616-619	4
β-strand	646	1	51
α-helix	647-662	16
β-strand	666-673	8	46
α-helix	686-696	11
α-helix	698-705	8
β-strand	711-714	4	52
α-helix	715-722	8
α-helix	723-725	3
α-helix	739-747	9
β-strand	757	1	52
β-strand	762-765	4	52
α-helix	767-780	14

Chains L and O: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	46-209	164

Chains N and P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	47-207	161

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-7	G, H, I, J, K, M	protein	776	Homo sapiens	P12883 (AlphaFold model)
Actin, alpha cardiac muscle 1	A, B, C, D, E, F	protein	371	Homo sapiens	P68032 (AlphaFold model)
Tropomyosin alpha-1 chain	L, N, O, P	protein	166	Homo sapiens	P09493 (AlphaFold model)

Sequence of entity 1 (G, H, I, J, K, M), FASTA

>8ZB7_1 Myosin-7 (chains G, H, I, J, K, M)
MAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEY
GKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTV
NPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKT
VNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG
KFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN
NPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFK
LKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATG
ALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL
QQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATD
MTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETV
VGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRST
HPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL
NPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERL

Sequence of entity 2 (A, B, C, D, E, F), FASTA

>8ZB7_2 Actin, alpha cardiac muscle 1 (chains A, B, C, D, E, F)
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF
ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD
LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD
GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDE
AGPSIVHRKCF

Sequence of entity 3 (L, N, O, P), FASTA

>8ZB7_3 Tropomyosin alpha-1 chain (chains L, N, O, P)
SLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQE
RLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE
VARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6

Primary citation

Cryo-EM structure of human left ventricle ATM complex. Li, D.N., Zhao, Q.Y., Liu, C. To be published.

Other PDB entries of the same protein (UniProt P12883 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5CJ1 2.1 Å, Crystal structure of the coiled coil of MYH7 residues 1526 to 1571 fused to Gp7
6PF2 2.17 Å, Crystal Structure of Amino Acids 1220-1276 of Human Beta Cardiac Myosin Fused to Gp7 and…
6PFP 2.2 Å, Crystal Structure of Amino Acids 1473-1536 of Human Beta Cardiac Myosin Fused to Gp7 and…
4PA0 2.25 Å, Omecamtiv Mercarbil binding site on the Human Beta-Cardiac Myosin Motor Domain
5CHX 2.3 Å, Crystal Structure of amino acids 1590-1657 of MYH7
5CJ0 2.3 Å, Crystal Structure of Amino Acids 1631-1692 of MYH7
5WME 2.3 Å, Crystal Structure of Amino Acids 1729-1786 of Human Beta Cardiac Myosin Fused to Gp7 as…
4XA4 2.33 Å, Crystal Structure of the coiled-coil surrounding Skip 3 of MYH7
9HTF 2.48 Å, Beta-cardiac myosin Y115H mutant motor domain in the pre-powerstroke state, MgADP.VO4 form
2FXO 2.5 Å, Structure of the human beta-myosin S2 fragment
5WJ7 2.5 Å, Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Xrcc4
4XA3 2.55 Å, Crystal structure of the coiled-coil surrounding Skip 2 of MYH7

Browse structure collections

About this viewer

MolViewer shows 8ZB7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.