1L2O: Myosin heavy chain

Scallop myosin S1-ADP-p-pdm in the actin-detached conformation. Determined by X-ray diffraction at 2.8 Å resolution. Released 30 Oct 2002.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Argopecten irradians
Chains: 3
Atoms: 8,339
Mol. weight: 131.32 kDa
Ligands: MG, PDM, ADP, CA
Released: 30 Oct 2002

Explore 1L2O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L2O contains 52 α-helices and 35 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, 29 β-strands

Element	Residues	Length	Sheet
β-strand	33-38	6	1
β-strand	42-50	9	1
β-strand	56-60	5	1
β-strand	65-69	5	1
β-strand	75-76	2	1
α-helix	77-79	3
α-helix	80-82	3
α-helix	96-108	13
β-strand	114	1	2
β-strand	121	1	2
β-strand	122-123	2	3
α-helix	134-140	7
α-helix	152-166	15
β-strand	169-175	7	4
α-helix	182-196	15
α-helix	215-221	7
α-helix	224-230	7
β-strand	231-234	4	5
β-strand	237-241	5	5
β-strand	244	1	6
β-strand	245-246	2	4
β-strand	248-251	4	7
β-strand	257-261	5	7
β-strand	265	1	6
α-helix	269-273	5
α-helix	283-288	6
α-helix	294-296	3
α-helix	297-300	4
α-helix	324-338	15
α-helix	342-360	19
α-helix	380-386	7
α-helix	391-397	7
β-strand	402	1	8
β-strand	411	1	8
α-helix	416-445	30
β-strand	454-455	2	7
β-strand	456	1	4
β-strand	459-460	2	4
α-helix	472-497	26
α-helix	514-524	11
α-helix	529-535	7
α-helix	544-548	5
α-helix	552-555	4
β-strand	563	1	9
β-strand	578-582	5	9
β-strand	585-589	5	9
α-helix	594-598	5
α-helix	604-611	8
α-helix	616-621	6
α-helix	647-660	14
β-strand	663-669	7	4
β-strand	670-671	2	3
α-helix	684-691	8
β-strand	710-712	3	10
α-helix	713-720	8
α-helix	736-745	10
β-strand	753-754	2	10
β-strand	759-762	4	10
α-helix	766-796	31
α-helix	799-813	15
α-helix	815-822	8
α-helix	825-832	8

Chain B: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	17-27	11
α-helix	37-46	10
α-helix	53-60	8
α-helix	69-78	10
α-helix	86-94	9
α-helix	106-114	9
α-helix	122-129	8
β-strand	134	1	11
β-strand	139	1	11
α-helix	141-148	8

Chain C: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-18	14
α-helix	20-22	3
β-strand	28-29	2	12
α-helix	30-35	6
α-helix	37-40	4
α-helix	46-52	7
β-strand	62-63	2	12
α-helix	65-77	13
α-helix	83-90	8
α-helix	91-93	3
β-strand	100-102	3	13
α-helix	103-112	10
α-helix	119-128	10
β-strand	138-140	3	13
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

>1L2O_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

>1L2O_2 MYOSIN REGULATORY LIGHT CHAIN (chains B)
ADKAASGVLTKLPQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAML
KEAPGPLNFTMFLSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNF
NKDEMRMTFKEAPVEGGKFDYVKFTAMIKGSGEEEA

Sequence of entity 3 (C), FASTA

>1L2O_3 MYOSIN ESSENTIAL LIGHT CHAIN (chains C)
PKLSQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGE
KSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDE
DVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGPYPDK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
PDM	4-[4-(2,5-dioxo-pyrrolidin-1-yl)-phenylamino]-4-hydroxy-butyric acid	C14 H16 N2 O5	1
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
CA	Calcium ion	Ca	1

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
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
1S5G 3.1 Å, Structure of Scallop myosin S1 reveals a novel nucleotide conformation

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