4LNZ: Human Myosin 5b globular domain

Crystal structure of human Myosin 5b globular domain. Determined by X-ray diffraction at 3.11 Å resolution. Released 25 Dec 2013.

Method
X-ray diffraction
Resolution
3.11 Å
Organism
Homo sapiens
Chains
1
Atoms
2,840
Mol. weight
45.11 kDa
Released
25 Dec 2013

Explore 4LNZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LNZ contains 16 α-helices and 2 β-strands across 1 chain. 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: 16 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand147111
α-helix1477-14815
α-helix1482-14865
α-helix1500-151415
α-helix1518-153720
α-helix1543-156321
α-helix1588-162033
α-helix1654-167017
α-helix1675-169622
α-helix1706-172621
α-helix1729-17313
α-helix1735-17373
α-helix1738-17469
α-helix1754-176310
α-helix1769-17779
α-helix1794-18007
α-helix1818-18203
β-strand184611

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Unconventional myosin-VbAprotein394Homo sapiensQ9ULV0 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4LNZ_1 Unconventional myosin-Vb (chains A)
GPLGSQRKEKDFQGMLEYHKEDEALLIRNLVTDLKPQMLSGTVPCLPAYILYMCIRHADY
TNDDLKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLSNTCRLLHCLKQYSGDEGFMTQNT
AKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGVLQPMIVSAMLENESIQGLSGVK
PTGYRKRSSSMADGDNSYCLEAIIRQMNAFHTVMCDQGLDPEIILQVFKQLFYMINAVTL
NNLLLRKDVCSWSTGMQLRYNISQLEEWLRGRNLHQSGAVQTMEPLIQAAQLLQLKKKTQ
EDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVAFIRTIQAQLQERNDPQQLLLDA
KHMFPVLFPFNPSSLTMDSIHIPACLNLEFLNEV

Primary citation

Structural insights into the globular tails of the human type v myosins myo5a, myo5b, and myo5c. Velvarska, H., Niessing, D. PLoS One (2013) 8:e82065-e82065. DOI 10.1371/journal.pone.0082065 · PubMed

Other PDB entries of the same protein (UniProt Q9ULV0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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