5JLH: Actin, cytoplasmic 2

Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Determined by electron microscopy at 3.9 Å resolution. Released 15 Jun 2016.

Method: Electron microscopy
Resolution: 3.9 Å
Organisms: Homo sapiens, Dictyostelium discoideum
Chains: 11
Atoms: 29,177
Mol. weight: 491.97 kDa
Ligands: MG, ADP
Released: 15 Jun 2016

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

Secondary structure: helices and β-sheets

5JLH contains 182 α-helices and 146 β-strands across 11 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	1
β-strand	15-20	6	1
β-strand	28-31	4	1
β-strand	34-37	4	2
α-helix	40-41	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	87-93	7
α-helix	97-99	3
β-strand	102-106	5	1
α-helix	112-124	13
β-strand	130-135	6	1
α-helix	136-144	9
β-strand	149-154	6	4
β-strand	159-164	6	4
β-strand	175-177	3	4
α-helix	181-193	13
α-helix	202-214	13
α-helix	222-228	7
β-strand	237-240	4	5
β-strand	246-249	4	5
α-helix	252-258	7
α-helix	259-261	3
α-helix	263-265	3
α-helix	273-283	11
α-helix	289-294	6
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	350-353	4
β-strand	356-357	2	1
α-helix	358-364	7
α-helix	368-372	5

Chains B, D and E: 22 helices, 18 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	78-86	9
α-helix	87-93	7
α-helix	97-99	3
β-strand	102-106	5	6
α-helix	112-124	13
β-strand	130-135	6	6
α-helix	136-143	8
β-strand	149-154	6	9
β-strand	159-164	6	9
β-strand	175-177	3	9
α-helix	181-193	13
α-helix	202-214	13
α-helix	222-228	7
β-strand	237-240	4	10
β-strand	246-249	4	10
α-helix	252-258	7
α-helix	259-261	3
α-helix	263-265	3
α-helix	273-283	11
α-helix	289-294	6
β-strand	296-299	4	9
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	9
α-helix	334-336	3
α-helix	337-347	11
α-helix	350-353	4
β-strand	356-357	2	6
α-helix	358-364	7
α-helix	368-372	5

Chain C: 22 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	11
β-strand	15-20	6	11
β-strand	28-31	4	11
β-strand	34-37	4	12
α-helix	40-41	2
β-strand	52-53	2	12
α-helix	56-59	4
β-strand	64-67	4	12
β-strand	70-71	2	13
β-strand	74-75	2	13
α-helix	78-86	9
α-helix	87-93	7
α-helix	97-99	3
β-strand	102-106	5	11
α-helix	112-124	13
β-strand	130-135	6	11
α-helix	136-143	8
β-strand	149-154	6	14
β-strand	159-164	6	14
β-strand	175-177	3	14
α-helix	181-193	13
α-helix	202-214	13
α-helix	222-228	7
β-strand	237-240	4	15
β-strand	246-249	4	15
α-helix	252-258	7
α-helix	259-261	3
α-helix	263-265	3
α-helix	273-283	11
α-helix	289-294	6
β-strand	296-299	4	14
α-helix	301-303	3
α-helix	308-319	12
β-strand	328-329	2	14
α-helix	334-336	3
α-helix	337-347	11
α-helix	350-353	4
β-strand	356-357	2	11
α-helix	358-364	7
α-helix	368-372	5

Chains F and G: 34 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	55-59	5	26
β-strand	65-74	10	26
β-strand	77-82	6	26
β-strand	88-92	5	26
α-helix	93-95	3
β-strand	97-98	2	26
β-strand	109	1	27
α-helix	110-112	3
α-helix	118-131	14
β-strand	135-138	4	27
β-strand	141-145	5	27
α-helix	150-151	2
α-helix	156-162	7
α-helix	174-188	15
β-strand	192-197	6	27
α-helix	204-218	15
α-helix	237-249	13
β-strand	250-251	2	28
β-strand	259-260	2	28
β-strand	264-270	7	27
β-strand	276-282	7	27
α-helix	289-292	4
β-strand	301	1	28
α-helix	302-310	9
α-helix	313-319	7
α-helix	324-326	3
α-helix	343-355	13
α-helix	359-374	16
β-strand	381	1	29
β-strand	390	1	29
α-helix	394-403	10
α-helix	408-416	9
β-strand	420-422	3	30
β-strand	425-427	3	30
α-helix	433-462	30
β-strand	472-479	8	27
α-helix	490-521	32
α-helix	530-533	4
α-helix	535-542	8
α-helix	548-549	2
α-helix	550-559	10
α-helix	565-575	11
β-strand	582-583	2	31
β-strand	594-597	4	31
β-strand	602-605	4	31
α-helix	610-614	5
β-strand	615	1	32
α-helix	620-627	8
α-helix	632-637	6
β-strand	669	1	32
α-helix	670-687	18
β-strand	689-696	8	27
α-helix	709-718	10
α-helix	721-728	8
β-strand	734-737	4	33
α-helix	738-745	8
α-helix	746-748	3
α-helix	761-770	10
α-helix	775-777	3
β-strand	778-780	3	33
β-strand	784-787	4	33
α-helix	791-815	25

Chains H, I, J and K: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	63-195	133

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, cytoplasmic 2	A, B, C, D, E	protein	374	Homo sapiens	P63261 (AlphaFold model)
Myosin-14,Alpha-actinin A	F, G	protein	1039	Homo sapiens, Dictyostelium discoideum	P05095 (AlphaFold model), Q7Z406 (AlphaFold model)
Tropomyosin alpha-3 chain	H, I, J, K	protein	135	Homo sapiens

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

>5JLH_1 Actin, cytoplasmic 2 (chains A, B, C, D, E)
EEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF

Sequence of entity 2 (F, G), FASTA

>5JLH_2 Myosin-14,Alpha-actinin A (chains F, G)
MAAVTMSVPGRKAPPRPGPVPEAAQPFLFTPRGPSAGGGPGSGTSPQVEWTARRLVWVPS
ELHGFEAAALRDEGEEEAEVELAESGRRLRLPRDQIQRMNPPKFSKAEDMAELTCLNEAS
VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEG
AYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQ
ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECS
FHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGFSHE
EIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRI
KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIA
GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDL
IERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYA
GKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG
RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG
VLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRV
GQSKIFFRAGVLAQLEEERASEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQS
FMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSAL
EKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQA
KLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVKSSA
ETYKNTLLAELERLQKIED

Sequence of entity 3 (H, I, J, K), FASTA

>5JLH_3 Tropomyosin alpha-3 chain (chains H, I, J, K)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXX

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	5
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	5

Primary citation

Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Ecken, J.V., Heissler, S.M., Pathan-Chhatbar, S. et al. Nature (2016) 534:724-728. DOI 10.1038/nature18295 · 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
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…
6CXJ 11.0 Å, Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C…

Browse more

5JLH is part of these collections:

Motor proteins and the cytoskeleton

About this viewer

MolViewer shows 5JLH 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.