1KWO: Myosin heavy chain

Scallop myosin S1-atpgammas-p-pdm in the actin-detached conformation. Determined by X-ray diffraction at 3.8 Å resolution. Released 20 Nov 2002.

Method: X-ray diffraction
Resolution: 3.8 Å
Organism: Argopecten irradians
Chains: 3
Atoms: 8,108
Mol. weight: 131.42 kDa
Ligands: CA, PDM, AGS, MG
Released: 20 Nov 2002

Explore 1KWO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KWO contains 50 α-helices and 38 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 A: 33 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	33-38	6	1
β-strand	42-51	10	1
β-strand	56-60	5	1
β-strand	68	1	1
β-strand	75	1	1
α-helix	76-79	4
α-helix	88-90	3
α-helix	98-107	10
β-strand	122-123	2	2
α-helix	134-139	6
α-helix	149-150	2
α-helix	152-164	13
β-strand	170-173	4	3
β-strand	175	1	4
α-helix	185-195	11
α-helix	224-230	7
β-strand	231-232	2	5
β-strand	240-241	2	5
β-strand	245	1	6
β-strand	248-252	5	3
β-strand	256-261	6	3
α-helix	269-273	5
α-helix	284-288	5
α-helix	294-297	4
α-helix	324-339	16
α-helix	342-358	17
β-strand	363	1	7
β-strand	374	1	7
α-helix	378-387	10
α-helix	391-399	9
β-strand	402	1	8
β-strand	411	1	8
α-helix	417-445	29
β-strand	454-459	6	3
β-strand	460	1	6
β-strand	470	1	9
α-helix	472-491	20
α-helix	515-518	4
α-helix	520-524	5
α-helix	529-533	5
α-helix	544-552	9
β-strand	578	1	9
β-strand	581	1	10
β-strand	586	1	10
β-strand	589	1	9
α-helix	596-598	3
α-helix	604-610	7
α-helix	616-621	6
α-helix	649-660	12
β-strand	664	1	3
β-strand	669	1	4
β-strand	670-671	2	2
α-helix	684-691	8
β-strand	709-712	4	11
α-helix	715-717	3
α-helix	721-723	3
α-helix	736-745	10
β-strand	753-755	3	11
β-strand	759-762	4	11
α-helix	767-798	32
α-helix	800-815	16
α-helix	819-822	4
α-helix	825-832	8

Chain B: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	15-27	13
β-strand	32	1	12
β-strand	34	1	12
α-helix	37-45	9
α-helix	50-52	3
α-helix	53-57	5
α-helix	75-78	4
α-helix	86-93	8
α-helix	106-114	9
α-helix	122-129	8
β-strand	134-135	2	13
β-strand	138-139	2	13
α-helix	141-148	8

Chain C: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-21	17
β-strand	28-29	2	14
α-helix	30-37	8
α-helix	46-51	6
β-strand	62-63	2	14
α-helix	65-72	8
α-helix	83-91	9
β-strand	101-102	2	15
α-helix	103-109	7
α-helix	119-129	11
β-strand	138-139	2	15
α-helix	141-150	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin heavy chain	A	protein	835	Argopecten irradians	P24733 (AlphaFold model)
Myosin regulatory light chain	B	protein	156	Argopecten irradians	P13543 (AlphaFold model)
Myosin essential light chain	C	protein	156	Argopecten irradians	P07291 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1KWO_1 MYOSIN HEAVY CHAIN (chains A)
MNIDFSDPDFQYLAVDRKKLMKEQTAAFDGKKNCWVPDEKEGFASAEIQSSKGDEITVKI
VADSSTRTVKKDDIQSMNPPKFEKLEDMANMTYLNEASVLYNLRSRYTSGLIYTYSGLFC
IAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGESGA
GKTENTKKVIMYLAKVACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNS
SRFGKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM
LVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGE
MKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVV
NSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYT
NERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFP
KADDKSFQDKLYQNHMGKNRMFTKPGKPTRPNQGPAHFELHHYAGNVPYSITGWLEKNKD
PINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTISAVHRESLNKLMKNL
YSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY
SILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFKAGVLGNLEEMRDERLSK
IISMFQAHIRGYLIRKAYKKLQDQRIGLSVIQRNIRKWLVLRNWQWWKLYSKVKP

Sequence of entity 2 (B), FASTA

>1KWO_2 MYOSIN REGULATORY LIGHT CHAIN (chains B)
ADKAASGVLTKLPQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAML
KEAPGPLNFTMFLSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNF
NKDEMRMTFKEAPVEGGKFDYVKFTAMIKGSGEEEA

Sequence of entity 3 (C), FASTA

>1KWO_3 MYOSIN ESSENTIAL LIGHT CHAIN (chains C)
PKLSQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGE
KSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDE
DVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGPYPDK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
PDM	4-[4-(2,5-dioxo-pyrrolidin-1-yl)-phenylamino]-4-hydroxy-butyric acid	C14 H16 N2 O5	1
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	1
MG	Magnesium ion	Mg	2

Primary citation

Crystallographic findings on the internally uncoupled and near-rigor states of myosin: Further insights into the mechanics of the motor. Himmel, D.M., Gourinath, S., Reshetnikova, L. et al. Proc Natl Acad Sci U S A (2002) 99:12645-12650. DOI 10.1073/pnas.202476799 · PubMed

Other PDB entries of the same protein (UniProt P24733 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WDC 2.0 Å, Scallop myosin regulatory domain
3JVT 2.1 Å, Calcium-bound Scallop Myosin Regulatory Domain (Lever Arm) with Reconstituted Complete…
1KK8 2.3 Å, Scallop myosin (S1-ADP-befx) in the actin-detached conformation
3BAS 2.3 Å, Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form
3BAT 2.3 Å, Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (P21)…
1B7T 2.5 Å, Myosin digested by papain
1QVI 2.54 Å, Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom…
3JTD 2.57 Å, Calcium-free Scallop Myosin Regulatory Domain with ELC-D19A Point Mutation
1SR6 2.75 Å, Structure of nucleotide-free scallop myosin S1
1L2O 2.8 Å, Scallop myosin S1-ADP-p-pdm in the actin-detached conformation
1SCM 2.8 Å, Structure of the regulatory domain of scallop myosin at 2.8 Å resolution
1KQM 3.0 Å, Scallop myosin S1-amppnp in the actin-detached conformation

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