6KU0: MyoVa-GTD

Crystal structure of MyoVa-GTD in complex with MICAL1-GTBM. Determined by X-ray diffraction at 1.6 Å resolution. Released 2 Sept 2020.

Method
X-ray diffraction
Resolution
1.6 Å
Organisms
Mus musculus, Homo sapiens
Chains
4
Atoms
7,043
Mol. weight
95.2 kDa
Released
2 Sept 2020

Explore 6KU0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6KU0 contains 54 α-helices and 10 β-strands across 4 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: 26 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand1475-147621
α-helix1479-14813
α-helix1482-14865
α-helix1487-14915
α-helix1498-15025
α-helix1506-152015
α-helix1524-154522
α-helix1549-156820
α-helix1573-15753
α-helix1581-15855
β-strand1591-159222
α-helix1594-162431
α-helix1625-16295
β-strand163313
β-strand163613
α-helix1637-16382
α-helix1659-167517
α-helix1680-170425
α-helix1711-173020
α-helix1734-17363
α-helix1739-17424
α-helix1743-17519
α-helix1759-176810
α-helix1774-178310
α-helix1784-17863
α-helix1792-17954
α-helix1796-180510
α-helix1823-18253
α-helix1836-18383
α-helix1843-18453
β-strand1851-185221
Chains B and D: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand804-80522
α-helix806-8094
α-helix810-8178
Chain C: 24 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand1475-147624
α-helix1479-14813
α-helix1482-14865
α-helix1487-14915
α-helix1495-15017
α-helix1506-152015
α-helix1524-154522
α-helix1549-156820
α-helix1573-15753
α-helix1581-15855
β-strand1591-159225
α-helix1594-162431
α-helix1625-16295
α-helix1659-167517
α-helix1680-170425
α-helix1711-173020
α-helix1734-17363
α-helix1739-17424
α-helix1743-175311
α-helix1759-176810
α-helix1774-178310
α-helix1792-17954
α-helix1796-180510
α-helix1823-18253
α-helix1836-18383
α-helix1843-18453
β-strand1851-185224

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Unconventional myosin-VaA, Cprotein389Mus musculusQ99104 (AlphaFold model)
Peptide from [F-actin]-monooxygenase MICAL1B, Dprotein27Homo sapiensQ8TDZ2 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>6KU0_1 Unconventional myosin-Va (chains A, C)
GPGSKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDD
QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQN
EHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGL
RKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLL
RKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEA
ICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSPQLLMDAKHIFP
VTFPFNPSSLALETIQIPASLGLGFIARV
Sequence of entity 2 (B, D), FASTA
>6KU0_2 Peptide from [F-actin]-monooxygenase MICAL1 (chains B, D)
GPGSQPTRRQIRLSSPERQRLSSLNLT

Primary citation

F-actin disassembly factor MICAL1 binding to Myosin Va mediates cargo unloading during cytokinesis. Niu, F., Sun, K., Wei, W. et al. Sci Adv (2020) 6. DOI 10.1126/sciadv.abb1307 · PubMed

Other PDB entries of the same protein (UniProt Q99104 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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