1KK8: Myosin Heavy Chain, Striated muscle

Scallop myosin (S1-ADP-befx) in the actin-detached conformation. Determined by X-ray diffraction at 2.3 Å resolution. Released 9 Oct 2002.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Argopecten irradians
Chains: 3
Atoms: 8,702
Mol. weight: 129.5 kDa
Ligands: CA, ADP, BEF, MG
Released: 9 Oct 2002

Explore 1KK8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KK8 contains 60 α-helices and 36 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: 41 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
β-strand	33-38	6	1
β-strand	42-52	11	1
β-strand	55-60	6	1
β-strand	66-70	5	1
α-helix	71-73	3
β-strand	75-76	2	1
α-helix	77-79	3
α-helix	80-82	3
β-strand	87	1	2
α-helix	88-90	3
α-helix	96-108	13
β-strand	113-116	4	2
β-strand	118-123	6	2
α-helix	134-140	7
α-helix	145-147	3
α-helix	152-162	11
α-helix	163-167	5
β-strand	169-175	7	2
α-helix	182-196	15
α-helix	198-200	3
α-helix	215-230	16
β-strand	231-232	2	3
β-strand	240-241	2	3
β-strand	244-251	8	2
β-strand	257-265	9	2
α-helix	269-272	4
β-strand	282	1	3
α-helix	283-288	6
α-helix	294-296	3
α-helix	297-300	4
α-helix	306-308	3
β-strand	319	1	4
β-strand	322	1	4
α-helix	324-337	14
α-helix	342-358	17
β-strand	363-364	2	5
β-strand	373-374	2	5
α-helix	378-387	10
α-helix	391-399	9
β-strand	402-403	2	6
β-strand	410-411	2	6
α-helix	416-446	31
β-strand	454-460	7	2
β-strand	470	1	7
α-helix	472-502	31
α-helix	514-524	11
α-helix	529-536	8
α-helix	544-555	12
β-strand	562-563	2	7
β-strand	578-582	5	7
β-strand	585-589	5	7
α-helix	594-598	5
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
α-helix	708	1
β-strand	709-712	4	8
α-helix	713-720	8
α-helix	721-723	3
α-helix	725-727	3
α-helix	735-746	12
α-helix	750-752	3
β-strand	753-755	3	8
β-strand	759-762	4	8
α-helix	766-822	57
α-helix	825-833	9
α-helix	834-836	3

Chain B: 10 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	15-27	13
α-helix	37-47	11
α-helix	50-52	3
α-helix	53-61	9
α-helix	69-77	9
α-helix	86-94	9
β-strand	104-105	2	9
α-helix	106-115	10
α-helix	119-121	3
α-helix	122-129	8
β-strand	134-135	2	9
β-strand	138-139	2	9
α-helix	141-148	8

Chain C: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-21	17
β-strand	28-29	2	10
α-helix	30-32	3
α-helix	33-39	7
α-helix	46-51	6
β-strand	62-63	2	10
α-helix	65-75	11
α-helix	83-91	9
β-strand	100-102	3	11
α-helix	103-112	10
α-helix	119-129	11
β-strand	138-140	3	11
α-helix	141-150	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin Heavy Chain, Striated muscle	A	protein	837	Argopecten irradians	P24733 (AlphaFold model)
Myosin Regulatory Light Chain, Striated adductor muscle	B	protein	139	Argopecten irradians	P13543 (AlphaFold model)
Myosin Essential Light Chain,Striated adductor muscle	C	protein	154	Argopecten irradians	P07291 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1KK8_1 Myosin Heavy Chain, Striated muscle (chains A)
MNIDFSDPDFQYLAVDRKKLMKEQTAAFDGKKNCWVPDEKEGFASAEIQSSKGDEITVKI
VADSSTRTVKKDDIQSMNPPKFEKLEDMANMTYLNEASVLYNLRSRYTSGLIYTYSGLFC
IAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGESGA
GKTENTKKVIMYLAKVACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNS
SRFGKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM
LVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGE
MKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVV
NSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYT
NERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFP
KADDKSFQDKLYQNHMGKNRMFTKPGKPTRPNQGPAHFELHHYAGNVPYSITGWLEKNKD
PINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTISAVHRESLNKLMKNL
YSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY
SILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFKAGVLGNLEEMRDERLSK
IISMFQAHIRGYLIRKAYKKLQDQRIGLSVIQRNIRKWLVLRNWQWWKLYSKVKPLL

Sequence of entity 2 (B), FASTA

>1KK8_2 Myosin Regulatory Light Chain, Striated adductor muscle (chains B)
PQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAMLKEAPGPLNFTMF
LSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNFNKDEMRMTFKEA
PVEGGKFDYVKFTAMIKGS

Sequence of entity 3 (C), FASTA

>1KK8_3 Myosin Essential Light Chain,Striated adductor muscle (chains C)
PKLSQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGE
KSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDE
DVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGPYP

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
BEF	Beryllium trifluoride ion	Be F3	1
MG	Magnesium ion	Mg	2

Water and common crystallization additives (GOL) are not listed.

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

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