2W4G: PDB entry 2W4G

Isometrically contracting insect asynchronous flight muscle quick frozen after a quick stretch step. Determined by electron microscopy. Released 25 Aug 2010.

Method: Electron microscopy
Organism: GALLUS GALLUS
Chains: 3
Atoms: 8,758
Mol. weight: 129.03 kDa
Released: 25 Aug 2010

Explore 2W4G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2W4G contains 61 α-helices and 39 β-strands across 3 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 B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	21-34	14
α-helix	44-53	10
α-helix	61-69	9
α-helix	77-87	11
α-helix	94-104	11
α-helix	111-113	3
α-helix	116-122	7
α-helix	132-139	8
α-helix	143-146	4
α-helix	150-159	10

Chain C: 12 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	9-15	7
α-helix	27-36	10
α-helix	45-46	2
α-helix	47-51	5
α-helix	54-58	5
α-helix	65-78	14
α-helix	79-82	4
α-helix	85-87	3
α-helix	89-92	4
β-strand	93-94	2	2
β-strand	99	1	3
β-strand	101-103	3	4
α-helix	104-113	10
α-helix	120-126	7
β-strand	136-138	3	4
β-strand	139	1	5
α-helix	140-147	8

Chain M: 39 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
α-helix	25-28	4
β-strand	37-41	5	6
β-strand	47-51	5	6
β-strand	52-55	4	7
β-strand	59-62	4	7
β-strand	70-73	4	7
α-helix	74-76	3
β-strand	77-78	2	6
β-strand	90	1	8
α-helix	91-93	3
α-helix	99-108	10
β-strand	116-119	4	8
β-strand	122-126	5	8
α-helix	133-135	3
α-helix	139-142	4
α-helix	155-165	11
α-helix	166-170	5
β-strand	173-179	7	8
α-helix	185-199	15
α-helix	221-233	13
β-strand	234-235	2	9
β-strand	243-244	2	9
β-strand	247-254	8	8
β-strand	260-262	3	8
β-strand	265-268	4	8
α-helix	272-275	4
β-strand	285	1	9
α-helix	286-291	6
α-helix	297-303	7
α-helix	309-311	3
α-helix	313-315	3
α-helix	327-340	14
α-helix	345-361	17
β-strand	366-368	3	10
α-helix	369	1
β-strand	375-377	3	10
α-helix	382-390	9
α-helix	394-402	9
β-strand	405	1	11
β-strand	414	1	11
α-helix	419-448	30
β-strand	457-465	9	8
β-strand	473	1	12
α-helix	475-505	31
α-helix	517-527	11
α-helix	532-539	8
α-helix	547-558	12
β-strand	559	1	13
β-strand	562	1	13
β-strand	565-566	2	12
β-strand	579-582	4	12
β-strand	587-590	4	12
α-helix	595-600	6
α-helix	605-612	8
α-helix	617-622	6
α-helix	650-665	16
β-strand	668-675	8	8
α-helix	688-698	11
α-helix	700-707	8
β-strand	714-716	3	14
α-helix	717-722	6
β-strand	723-724	2	2
α-helix	725-727	3
β-strand	732	1	5
α-helix	733-736	4
β-strand	740	1	3
α-helix	742-747	6
β-strand	758-761	4	14
β-strand	764-767	4	14
α-helix	771-778	8
α-helix	781-826	46
α-helix	830-838	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin regulatory light chain 2, skeletal muscle isoform	B	protein	150	GALLUS GALLUS	P02609 (AlphaFold model)
Myosin light chain 3, skeletal muscle isoform	C	protein	145	GALLUS GALLUS	P02605 (AlphaFold model)
Myosin heavy chain, skeletal muscle, adult	M	protein	840	GALLUS GALLUS	P13538 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>2W4G_1 MYOSIN REGULATORY LIGHT CHAIN 2, SKELETAL MUSCLE ISOFORM (chains B)
NVFSMFDQTQIQDFKEAFTVIDQNRDGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASG
PINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTQCDRFTPEEI
KNMWAAFPPDVAGNVDYKNICYVITHGEDK

Sequence of entity 2 (C), FASTA

>2W4G_2 MYOSIN LIGHT CHAIN 3, SKELETAL MUSCLE ISOFORM (chains C)
DEINDFKEAFLLFDRTGDAKITLSQVGDIVRALGQNPTNAEINKILGNPSKEEMNAKKIT
FEEFLPMLQAAANNKDQGTFEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMTEEEVE
ELMKGQEDSNGCINYEAFVKHIMSV

Sequence of entity 3 (M), FASTA

>2W4G_3 MYOSIN HEAVY CHAIN, SKELETAL MUSCLE, ADULT (chains M)
DAEMAAFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVHPKESFVKGTIQSKEGGKVTVK
TEGGETLTVKEDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFC
VTVNPYKWLPVYNPKVVLAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGA
GKTVNTKRVIQYFATIAASGEKKKEEQSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNS
SRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLPAERSYHIFYQIMSNKKPELIDML
LITTNPYDYHYVSQGEITVPSIDDQEELMATDSAIDILGFSADEKTAIYKLTGAVMHYGN
LKFKQKQREEQAEPDGTEVADKAAYLMGLNSAELLKALCYPRVKVGNEFVTKGQTVSQVH
NSVGALAKAVYEKMFLWMVIRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT
NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFP
KATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLEKNKDPL
NETVIGLYQKSSVKTLALLFATYGGEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMAN
LRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRVLYADFKQR
YRVLNASAIPEGQFMDSKKASEKLLGSIDVDHTQYRFGHTKVFFKAGLLGLLEEMRDDKL
AEIITRTQARCRGFLMRVEYRRMVERRESIFCIQYNVRSFMNVKHWPWMKLFFKIKPLLK

Primary citation

Electron Tomography of Cryofixed, Isometrically Contracting Insect Flight Muscle Reveals Novel Actin-Myosin Interactions. Wu, S., Liu, J., Reedy, M.C. et al. PLoS One (2010) 5:12643. DOI 10.1371/JOURNAL.PONE.0012643 · PubMed

Other PDB entries of the same protein (UniProt P02609 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2MYS 2.8 Å, Myosin subfragment-1, alpha carbon coordinates only for the two light chains
1I84 20.0 Å, cryo-EM structure of the heavy meromyosin subfragment of chicken gizzard smooth muscle…
1M8Q 70.0 Å, Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle
1MVW 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O18 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O19 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1A 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1B 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1C 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1D 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1E 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1F 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle

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