3GN4: Myosin lever arm

Myosin lever arm. Determined by X-ray diffraction at 2.7 Å resolution. Released 8 Sept 2009.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Sus scrofa, Drosophila melanogaster
Chains: 6
Atoms: 6,343
Mol. weight: 102.51 kDa
Ligands: MG, CA
Released: 8 Sept 2009

Explore 3GN4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GN4 contains 42 α-helices and 16 β-strands across 6 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	774-848	75
α-helix	866-885	20
α-helix	892-912	21

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	1
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	1
α-helix	65-71	7
α-helix	80-92	13
β-strand	99-100	2	2
α-helix	102-111	10
α-helix	118-128	11
β-strand	136-137	2	2
α-helix	138-146	9

Chain D: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-28	3	3
α-helix	31-38	8
α-helix	45-52	8
β-strand	62-64	3	3
α-helix	65-74	10
α-helix	75-77	3
α-helix	82-90	9
β-strand	99-101	3	4
α-helix	102-111	10
α-helix	115-117	3
α-helix	118-128	11
β-strand	135-137	3	4
α-helix	138-145	8

Chain E: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	776-846	71
α-helix	868-887	20
α-helix	892-900	9
α-helix	904-908	5

Chain F: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	27	1	5
α-helix	29-38	10
α-helix	45-55	11
β-strand	63	1	5
α-helix	65-71	7
α-helix	80-92	13
β-strand	99-100	2	6
α-helix	102-111	10
α-helix	118-128	11
β-strand	136-137	2	6
α-helix	138-145	8

Chain H: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-28	3	7
α-helix	29-38	10
α-helix	45-55	11
β-strand	62-64	3	7
α-helix	65-77	13
α-helix	83-90	8
β-strand	100-101	2	8
α-helix	102-111	10
α-helix	115-117	3
α-helix	118-126	9
β-strand	135-136	2	8
α-helix	138-144	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-VI	A, E	protein	148	Sus scrofa	Q29122 (AlphaFold model)
Calmodulin	B, D, F, H	protein	149	Drosophila melanogaster	P62152 (AlphaFold model)

Sequence of entity 1 (A, E), FASTA

>3GN4_1 Myosin-VI (chains A, E)
MKSDPDHLAELVKRVNHWLICSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLC
KRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKQEMSKQVKDLEISIDALMAKIKSTM
MTREQIQKEYDALVKSSAVLLSALQKKK

Sequence of entity 2 (B, D, F, H), FASTA

>3GN4_2 Calmodulin (chains B, D, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVTMMTSK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	8
CA	Calcium ion	Ca	8

Primary citation

Myosin VI dimerization triggers an unfolding of a three-helix bundle in order to extend its reach. Mukherjea, M., Llinas, P., Kim, H. et al. Mol Cell (2009) 35:305-315. DOI 10.1016/j.molcel.2009.07.010 · PubMed

Other PDB entries of the same protein (UniProt Q29122 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2V26 1.75 Å, Myosin VI (MD) pre-powerstroke state (Mg.ADP.VO4)
4DBR 1.95 Å, Myosin VI D179Y (MD) pre-powerstroke state
2X51 2.2 Å, M6 delta Insert1
3L9I 2.2 Å, Myosin VI nucleotide-free (mdinsert2) L310G mutant crystal structure
4DBP 2.2 Å, Myosin VI nucleotide-free (MDINSERT2) D179Y crystal structure
5O2L 2.2 Å, Myosin VI motor domain in the Pre-Transition State
2VB6 2.3 Å, Myosin VI (MD-insert2-CaM, Delta Insert1) Post-rigor state (crystal form 2)
2BKH 2.4 Å, Myosin VI nucleotide-free (MDInsert2) crystal structure
2VAS 2.4 Å, Myosin VI (MD-insert2-CaM, Delta-Insert1) Post-rigor state
4ANJ 2.6 Å, MYOSIN VI (MDinsert2-GFP fusion) PRE-POWERSTROKE STATE (MG.ADP.AlF4)
4DBQ 2.6 Å, MYOSIN VI D179Y (MD-INSERT2-CAM, DELTA-INSERT1) post-rigor state
2BKI 2.9 Å, Myosin VI nucleotide-free (MDinsert2-IQ) crystal structure

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