3WB8: MyoVa-GTD
Crystal Structure of MyoVa-GTD. Determined by X-ray diffraction at 2.5 Å resolution. Released 10 Jul 2013.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Mus musculus
- Chains
- 8
- Atoms
- 23,277
- Mol. weight
- 370.34 kDa
- Released
- 10 Jul 2013
Explore 3WB8 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3WB8 contains 184 α-helices and 24 β-strands across 8 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: 22 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 1 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| β-strand | 1591 | 1 | 2 |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1676 | 18 | |
| α-helix | 1680-1704 | 25 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1738-1753 | 16 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1793-1795 | 3 | |
| α-helix | 1796-1805 | 10 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 1 |
Chain B: 22 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 3 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| β-strand | 1591 | 1 | 4 |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1702 | 23 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1738-1741 | 4 | |
| α-helix | 1743-1753 | 11 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1796-1805 | 10 | |
| α-helix | 1823-1826 | 4 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 3 |
Chain C: 24 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 5 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1521 | 16 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1704 | 25 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1739-1742 | 4 | |
| α-helix | 1743-1753 | 11 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1793-1795 | 3 | |
| α-helix | 1796-1806 | 11 | |
| β-strand | 1811 | 1 | 2 |
| α-helix | 1823-1825 | 3 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 5 |
Chain D: 25 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 6 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1584 | 4 | |
| β-strand | 1591 | 1 | 7 |
| α-helix | 1594-1624 | 31 | |
| α-helix | 1625-1629 | 5 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1702 | 23 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1738-1741 | 4 | |
| α-helix | 1743-1753 | 11 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1793-1795 | 3 | |
| α-helix | 1796-1805 | 10 | |
| α-helix | 1807-1809 | 3 | |
| β-strand | 1811 | 1 | 8 |
| α-helix | 1823-1825 | 3 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 6 |
Chain E: 24 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 9 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| β-strand | 1591 | 1 | 10 |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1676 | 18 | |
| α-helix | 1680-1704 | 25 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1740-1742 | 3 | |
| α-helix | 1743-1753 | 11 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1796-1805 | 10 | |
| α-helix | 1807-1809 | 3 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| α-helix | 1850 | 1 | |
| β-strand | 1851-1852 | 2 | 9 |
Chain F: 22 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 11 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1676 | 18 | |
| α-helix | 1680-1704 | 25 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1738-1741 | 4 | |
| α-helix | 1743-1751 | 9 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1796-1806 | 11 | |
| β-strand | 1811 | 1 | 10 |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 11 |
Chain G: 23 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 12 |
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1498-1502 | 5 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1545 | 22 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| β-strand | 1591 | 1 | 8 |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1704 | 25 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1740-1742 | 3 | |
| α-helix | 1743-1753 | 11 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1793-1795 | 3 | |
| α-helix | 1796-1806 | 11 | |
| β-strand | 1811 | 1 | 7 |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 12 |
Chain H: 22 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1479-1481 | 3 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1487-1491 | 5 | |
| α-helix | 1499-1502 | 4 | |
| α-helix | 1506-1520 | 15 | |
| α-helix | 1524-1544 | 21 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1585 | 5 | |
| α-helix | 1594-1623 | 30 | |
| α-helix | 1624-1629 | 6 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1704 | 25 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1730 | 20 | |
| α-helix | 1739-1742 | 4 | |
| α-helix | 1743-1751 | 9 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1796-1806 | 11 | |
| β-strand | 1811 | 1 | 4 |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Unconventional myosin-Va | A, B, C, D, E, F, G, H | protein | 404 | Mus musculus | Q99104 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>3WB8_1 Unconventional myosin-Va (chains A, B, C, D, E, F, G, H)
HHHHHHSSGLGVLFQGPGSKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLIPGLPAY
ILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQY
SGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLE
HETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQ
MFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAA
QLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDR
KDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFIARV
Primary citation
Structural basis of cargo recognitions for class V myosins. Wei, Z., Liu, X., Yu, C. et al. Proc Natl Acad Sci U S A (2013) 110:11314-11319. DOI 10.1073/pnas.1306768110 · PubMed
Other PDB entries of the same protein (UniProt Q99104 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6KU0 1.6 Å, Crystal structure of MyoVa-GTD in complex with MICAL1-GTBM
- 4KP3 2.4 Å, Crystal Structure of MyoVa-GTD in Complex with Two Cargos
- 2IX7 2.5 Å, Structure of apo-calmodulin bound to unconventional myosin V
- 4ZLK 2.5 Å, Crystal structure of mouse myosin-5a in complex with calcium-bound calmodulin
- 8RBF 4.2 Å, CryoEM structure of the post-powerstroke actomyosin-5a complex
- 8R9V 4.4 Å, CryoEM structure of the primed actomyosin-5a complex
- 7YV9 4.78 Å, Cryo-EM structure of full-length Myosin Va in the autoinhibited state
- 8RBG 4.9 Å, CryoEM structure of primed myosin-5a (ADP-Pi state)
- 8OF8 7.5 Å, Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)
Browse structure collections
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