Crystal structure of Myo5b globular tail domain in complex with inactive Rab11a. Determined by X-ray diffraction at 2.55 Å resolution. Released 20 Nov 2013.
Explore 4LWZ in 3D Show helices and sheets RCSB PDB PDBe
4LWZ contains 63 α-helices and 16 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-17 | 8 | 1 |
| α-helix | 24-33 | 10 | |
| α-helix | 41-43 | 3 | |
| β-strand | 46-55 | 10 | 1 |
| β-strand | 58-67 | 10 | 1 |
| α-helix | 75-81 | 7 | |
| β-strand | 86-92 | 7 | 1 |
| α-helix | 96-100 | 5 | |
| α-helix | 102-112 | 11 | |
| β-strand | 118-124 | 7 | 1 |
| α-helix | 129-131 | 3 | |
| α-helix | 136-145 | 10 | |
| β-strand | 149-152 | 4 | 1 |
| α-helix | 161-172 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1470-1471 | 2 | 2 |
| α-helix | 1474-1476 | 3 | |
| α-helix | 1477-1481 | 5 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1490-1493 | 4 | |
| α-helix | 1500-1514 | 15 | |
| α-helix | 1518-1538 | 21 | |
| α-helix | 1543-1562 | 20 | |
| α-helix | 1567-1569 | 3 | |
| α-helix | 1575-1578 | 4 | |
| α-helix | 1588-1618 | 31 | |
| α-helix | 1619-1623 | 5 | |
| α-helix | 1654-1670 | 17 | |
| α-helix | 1675-1697 | 23 | |
| α-helix | 1706-1725 | 20 | |
| α-helix | 1734-1737 | 4 | |
| α-helix | 1738-1746 | 9 | |
| α-helix | 1754-1763 | 10 | |
| α-helix | 1769-1777 | 9 | |
| α-helix | 1787-1790 | 4 | |
| α-helix | 1791-1800 | 10 | |
| α-helix | 1801-1803 | 3 | |
| α-helix | 1818-1820 | 3 | |
| α-helix | 1822-1824 | 3 | |
| α-helix | 1831-1833 | 3 | |
| α-helix | 1838-1840 | 3 | |
| β-strand | 1846-1847 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-17 | 6 | 3 |
| α-helix | 24-33 | 10 | |
| α-helix | 40-42 | 3 | |
| β-strand | 46-54 | 9 | 3 |
| β-strand | 59-67 | 9 | 3 |
| α-helix | 78-81 | 4 | |
| β-strand | 86-92 | 7 | 3 |
| α-helix | 96-100 | 5 | |
| α-helix | 102-112 | 11 | |
| β-strand | 118-124 | 7 | 3 |
| α-helix | 129-131 | 3 | |
| α-helix | 136-146 | 11 | |
| β-strand | 149-152 | 4 | 3 |
| α-helix | 161-171 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1470-1471 | 2 | 4 |
| α-helix | 1474-1476 | 3 | |
| α-helix | 1477-1481 | 5 | |
| α-helix | 1482-1486 | 5 | |
| α-helix | 1490-1493 | 4 | |
| α-helix | 1500-1514 | 15 | |
| α-helix | 1518-1538 | 21 | |
| α-helix | 1543-1562 | 20 | |
| α-helix | 1567-1570 | 4 | |
| α-helix | 1577-1580 | 4 | |
| α-helix | 1588-1613 | 26 | |
| α-helix | 1654-1670 | 17 | |
| α-helix | 1675-1694 | 20 | |
| α-helix | 1706-1725 | 20 | |
| α-helix | 1733-1736 | 4 | |
| α-helix | 1738-1746 | 9 | |
| α-helix | 1754-1763 | 10 | |
| α-helix | 1769-1777 | 9 | |
| α-helix | 1791-1800 | 10 | |
| α-helix | 1818-1820 | 3 | |
| α-helix | 1822-1824 | 3 | |
| α-helix | 1831-1833 | 3 | |
| α-helix | 1838-1840 | 3 | |
| β-strand | 1846-1847 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras-related protein Rab-11A | A, C | protein | 177 | Homo sapiens | P62491 (AlphaFold model) |
| Unconventional myosin-Vb | B, D | protein | 427 | Homo sapiens | Q9ULV0 (AlphaFold model) |
>4LWZ_1 Ras-related protein Rab-11A (chains A, C) MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTI KAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIM LVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVS
>4LWZ_2 Unconventional myosin-Vb (chains B, D) MRSETMSYYHHHHHHDYDIPTTENLYFQGAMGSMQVTVQRKEKDFQGMLEYHKEDEALLI RNLVTDLKPQMLSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLTSTINGIKKVLKKHND DFEMTSFWLSNTCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQI YQQLIKIAEGVLQPMIVSAMLENESIQGLSGVKPTGYRKRSSSMADGDNSYCLEAIIRQM NAFHTVMCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEE WLRGRNLHQSGAVQTMEPLIQAAQLLQLKKKTQEDAEAICSLCTSLSTQQIVKILNLYTP LNEFEERVTVAFIRTIQAQLQERNDPQQLLLDAKHMFPVLFPFNPSSLTMDSIHIPACLN LEFLNEV
Structural basis of myosin V Rab GTPase-dependent cargo recognition. Pylypenko, O., Attanda, W., Gauquelin, C. et al. Proc Natl Acad Sci U S A (2013) 110:20443-20448. DOI 10.1073/pnas.1314329110 · PubMed
Other PDB entries of the same protein (UniProt P62491 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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