1KK7: Scallop myosin in the near rigor conformation

Scallop myosin in the near rigor conformation. Determined by X-ray diffraction at 3.2 Å resolution. Released 9 Oct 2002.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Argopecten irradians
Chains: 3
Atoms: 8,147
Mol. weight: 130.92 kDa
Ligands: MG, CA
Released: 9 Oct 2002

Explore 1KK7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KK7 contains 56 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: 35 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	18-21	4
β-strand	33-35	3	1
β-strand	38	1	2
β-strand	42	1	2
β-strand	45-51	7	1
β-strand	56-60	5	1
β-strand	67-69	3	1
β-strand	75-76	2	1
α-helix	80-82	3
β-strand	87	1	3
α-helix	88-90	3
α-helix	96-109	14
β-strand	113-116	4	3
β-strand	118-123	6	3
α-helix	130-132	3
α-helix	134-139	6
α-helix	152-162	11
α-helix	163-167	5
β-strand	170-171	2	4
β-strand	174-176	3	3
α-helix	182-193	12
α-helix	194-196	3
α-helix	215-230	16
β-strand	244-245	2	5
β-strand	249-251	3	6
β-strand	257-260	4	6
β-strand	264-265	2	5
α-helix	269-271	3
α-helix	285-288	4
α-helix	294-296	3
α-helix	297-301	5
α-helix	327-336	10
α-helix	342-358	17
β-strand	363	1	7
β-strand	371	1	8
β-strand	374	1	7
α-helix	378-387	10
α-helix	391-399	9
β-strand	415	1	8
α-helix	416-446	31
β-strand	454-455	2	6
β-strand	456-457	2	4
β-strand	460	1	3
α-helix	472-502	31
α-helix	516-524	9
α-helix	529-533	5
α-helix	544-555	12
β-strand	562-563	2	9
β-strand	579-582	4	9
β-strand	585-588	4	9
α-helix	594-598	5
α-helix	606-611	6
α-helix	616-621	6
α-helix	645-660	16
β-strand	664	1	4
β-strand	668-671	4	3
α-helix	684-694	11
α-helix	700-704	5
β-strand	710-712	3	10
α-helix	713-717	5
α-helix	736-745	10
α-helix	750-752	3
β-strand	753-755	3	10
β-strand	759-762	4	10
α-helix	766-821	56
α-helix	834-836	3

Chain Y: 11 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	14-25	12
α-helix	39-42	4
α-helix	44-46	3
α-helix	49-52	4
α-helix	53-61	9
α-helix	75-80	6
α-helix	86-92	7
α-helix	93-96	4
β-strand	104-105	2	11
α-helix	106-114	9
α-helix	122-128	7
β-strand	134-135	2	11
β-strand	138-139	2	11
α-helix	141-149	9

Chain Z: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-20	16
β-strand	29	1	12
α-helix	30-32	3
α-helix	33-40	8
α-helix	46-50	5
β-strand	62	1	12
α-helix	65-74	10
α-helix	83-91	9
β-strand	101-102	2	13
α-helix	103-112	10
α-helix	119-125	7
α-helix	126-130	5
β-strand	138-139	2	13
α-helix	142-150	9

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	Y	protein	156	Argopecten irradians	P13543 (AlphaFold model)
Myosin essential light chain, striated adductor muscle	Z	protein	156	Argopecten irradians	P07291 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1KK7_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 (Y), FASTA

>1KK7_2 MYOSIN REGULATORY LIGHT CHAIN, STRIATED ADDUCTOR MUSCLE (chains Y)
ADKAASGVLTKLPQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAML
KEAPGPLNFTMFLSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNF
NKDEMRMTFKEAPVEGGKFDYVKFTAMIKGSGEEEA

Sequence of entity 3 (Z), FASTA

>1KK7_3 MYOSIN ESSENTIAL LIGHT CHAIN, STRIATED ADDUCTOR MUSCLE (chains Z)
PKLSQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGE
KSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDE
DVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGPYPDK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
CA	Calcium ion	Ca	1

Water and common crystallization additives (SO4) 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…
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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