2X51: M6 delta Insert1

M6 delta Insert1. Determined by X-ray diffraction at 2.2 Å resolution. Released 26 Jan 2011.

Method
X-ray diffraction
Resolution
2.2 Å
Organisms
SUS SCROFA, DROSOPHILA MELANOGASTER
Chains
2
Atoms
7,401
Mol. weight
107.72 kDa
Ligands
CA
Released
26 Jan 2011

Explore 2X51 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2X51 contains 45 α-helices and 31 β-strands across 2 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: 37 helices, 27 β-strands

ElementResiduesLengthSheet
β-strand7-1151
β-strand15-1951
β-strand28-3032
β-strand42-4432
α-helix45-473
β-strand49-5021
β-strand6113
α-helix62-643
α-helix70-8213
β-strand87-9043
β-strand93-9753
α-helix109-1146
α-helix118-1192
α-helix127-14115
β-strand145-15063
α-helix157-17216
α-helix178-19316
β-strand194-19524
β-strand203-20424
β-strand207-21483
β-strand220-22893
α-helix233-2353
β-strand24514
α-helix246-2549
α-helix257-2626
α-helix268-2703
α-helix313-32614
α-helix331-34717
β-strand352-35435
β-strand362-36435
α-helix366-3683
α-helix369-37810
α-helix383-3919
β-strand392-39326
β-strand409-41026
α-helix413-44129
β-strand450-45673
β-strand46617
α-helix468-49831
α-helix512-5198
α-helix525-5339
α-helix540-55011
β-strand557-55827
α-helix560-5623
β-strand576-58167
β-strand584-58967
α-helix593-5964
α-helix600-6023
α-helix603-6108
α-helix615-6206
α-helix643-65917
β-strand662-66983
α-helix682-69110
α-helix694-7018
β-strand707-71048
α-helix711-7188
α-helix719-7213
α-helix724-7274
α-helix731-74212
β-strand749-75138
β-strand755-75848
α-helix762-7709
α-helix774-7829
α-helix785-81430
Chain B: 8 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix7-2014
β-strand2819
α-helix30-3910
α-helix46-549
β-strand6419
α-helix66-738
α-helix82-9312
β-strand100-101210
α-helix103-11210
α-helix119-12911
β-strand137-138210
α-helix139-1468

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin-VIAprotein789SUS SCROFAQ29122 (AlphaFold model)
CalmodulinBprotein149DROSOPHILA MELANOGASTERP62152 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2X51_1 MYOSIN-VI (chains A)
MEDGKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVE
DNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSL
GTMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDD
RIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
EERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGGSLKDPLLDDHGDFIRMCTAMKK
IGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQALEYCAELLGLDQDDL
RVSLTTRVMLTTAGGAKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFE
TSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEV
HYVDNQDCIDLIEARLVGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSKLA
IHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTN
NNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQIL
SQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPDKLARLDPRLFCKALFKALGLNE
IDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLICSRWKKVQWCSLSVIKL
KNKIKYRAE
Sequence of entity 2 (B), FASTA
>2X51_2 CALMODULIN (chains B)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVTMMTSK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa3

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

Role of Insert-1 of Myosin Vi in Modulating Nucleotide Affinity. Pylypenko, O., Song, L., Squires, G. et al. J Biol Chem (2011) 286:11716. DOI 10.1074/JBC.M110.200626 · PubMed

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

Browse structure collections

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