1KQM: MYOSIN heavy chain

Scallop myosin S1-amppnp in the actin-detached conformation. Determined by X-ray diffraction at 3.0 Å resolution. Released 20 Nov 2002.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Argopecten irradians
Chains: 3
Atoms: 8,276
Mol. weight: 131.11 kDa
Ligands: MG, CA, ANP
Released: 20 Nov 2002

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

Secondary structure: helices and β-sheets

1KQM contains 54 α-helices and 34 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: 38 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	33-37	5	1
β-strand	43-52	10	1
β-strand	55-60	6	1
β-strand	67	1	1
β-strand	70	1	1
β-strand	75	1	1
α-helix	80-82	3
β-strand	87	1	2
α-helix	96-107	12
β-strand	113-115	3	2
β-strand	119-123	5	2
α-helix	130-132	3
α-helix	134-140	7
α-helix	149-150	2
α-helix	152-166	15
β-strand	169-176	8	2
α-helix	182-193	12
α-helix	194-196	3
α-helix	215-219	5
α-helix	222-230	9
β-strand	232	1	3
β-strand	240	1	3
β-strand	244-250	7	2
β-strand	251	1	4
β-strand	257	1	4
β-strand	261-265	5	2
α-helix	270-272	3
β-strand	282	1	3
α-helix	283-287	5
α-helix	294-296	3
α-helix	297-300	4
α-helix	324-337	14
α-helix	342-358	17
α-helix	380-382	3
α-helix	383-387	5
α-helix	391-397	7
β-strand	403	1	5
β-strand	410	1	5
α-helix	418-446	29
β-strand	455-460	6	2
α-helix	473-490	18
α-helix	493-496	4
α-helix	497-499	3
α-helix	517-524	8
α-helix	529-533	5
α-helix	546-555	10
β-strand	578	1	6
β-strand	581-583	3	7
β-strand	585-586	2	7
β-strand	589	1	6
α-helix	594-597	4
α-helix	604-611	8
α-helix	616-621	6
α-helix	645-660	16
β-strand	663-671	9	2
α-helix	684-691	8
β-strand	711-712	2	8
α-helix	713-720	8
α-helix	721-723	3
α-helix	740-744	5
β-strand	753-755	3	8
β-strand	759-762	4	8
α-helix	766-796	31
α-helix	799-814	16
α-helix	821-823	3
α-helix	825-832	8

Chain B: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	15-27	13
α-helix	37-44	8
α-helix	53-60	8
α-helix	69-77	9
α-helix	94-96	3
β-strand	104-105	2	9
α-helix	109-115	7
α-helix	122-129	8
β-strand	138-139	2	9
α-helix	141-146	6

Chain C: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
β-strand	28-29	2	10
α-helix	30-39	10
α-helix	46-49	4
β-strand	62-63	2	10
α-helix	65-74	10
α-helix	91-93	3
β-strand	101-102	2	11
α-helix	103-112	10
α-helix	119-128	10
β-strand	138-139	2	11
α-helix	141-149	9

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

>1KQM_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

>1KQM_2 MYOSIN REGULATORY LIGHT CHAIN (chains B)
ADKAASGVLTKLPQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAML
KEAPGPLNFTMFLSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNF
NKDEMRMTFKEAPVEGGKFDYVKFTAMIKGSGEEEA

Sequence of entity 3 (C), FASTA

>1KQM_3 MYOSIN ESSENTIAL LIGHT CHAIN (chains C)
PKLSQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGE
KSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDE
DVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGPYPDK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
CA	Calcium ion	Ca	1
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	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
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
1S5G 3.1 Å, Structure of Scallop myosin S1 reveals a novel nucleotide conformation

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