4KP3: MyoVa-GTD
Crystal Structure of MyoVa-GTD in Complex with Two Cargos. Determined by X-ray diffraction at 2.4 Å resolution. Released 10 Jul 2013.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organism
- Mus musculus
- Chains
- 6
- Atoms
- 7,359
- Mol. weight
- 125.19 kDa
- Released
- 10 Jul 2013
Explore 4KP3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4KP3 contains 61 α-helices and 10 β-strands across 6 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: 23 helices, 5 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 | 1524-1544 | 21 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1575 | 3 | |
| α-helix | 1581-1584 | 4 | |
| β-strand | 1591-1592 | 2 | 2 |
| α-helix | 1594-1624 | 31 | |
| α-helix | 1625-1629 | 5 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1704 | 25 | |
| β-strand | 1710 | 1 | 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 | |
| β-strand | 1785 | 1 | 3 |
| α-helix | 1793-1795 | 3 | |
| α-helix | 1796-1805 | 10 | |
| α-helix | 1823-1825 | 3 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 1 |
Chain B: 24 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1475-1476 | 2 | 4 |
| 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 | 1524-1544 | 21 | |
| α-helix | 1549-1568 | 20 | |
| α-helix | 1573-1576 | 4 | |
| α-helix | 1581-1584 | 4 | |
| β-strand | 1591-1592 | 2 | 5 |
| α-helix | 1594-1627 | 34 | |
| α-helix | 1659-1675 | 17 | |
| α-helix | 1680-1703 | 24 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1711-1729 | 19 | |
| α-helix | 1739-1742 | 4 | |
| α-helix | 1743-1751 | 9 | |
| α-helix | 1759-1768 | 10 | |
| α-helix | 1774-1783 | 10 | |
| α-helix | 1793-1795 | 3 | |
| α-helix | 1796-1805 | 10 | |
| α-helix | 1806-1808 | 3 | |
| α-helix | 1823-1825 | 3 | |
| α-helix | 1836-1838 | 3 | |
| α-helix | 1843-1845 | 3 | |
| β-strand | 1851-1852 | 2 | 4 |
Chain C: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-19 | 4 | |
| α-helix | 23-25 | 3 | |
| α-helix | 28-43 | 16 | |
| α-helix | 49-71 | 23 | |
| α-helix | 74-93 | 20 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-19 | 4 | |
| α-helix | 23-25 | 3 | |
| α-helix | 28-43 | 16 | |
| α-helix | 49-94 | 46 | |
Chain E: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 185-186 | 2 | |
| β-strand | 187-188 | 2 | 2 |
| α-helix | 193-195 | 3 | |
Chain F: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 185-186 | 2 | |
| β-strand | 187-188 | 2 | 5 |
| α-helix | 189-190 | 2 | |
| α-helix | 193-195 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Unconventional myosin-Va | A, B | protein | 404 | Mus musculus | Q99104 (AlphaFold model) |
| RILP-like protein 2 | C, D | protein | 103 | Mus musculus | Q99LE1 (AlphaFold model) |
| Melanophilin | E, F | protein | 43 | Mus musculus | Q91V27 (AlphaFold model) |
Sequence of entity 1 (A, B), FASTA
>4KP3_1 Unconventional myosin-Va (chains A, B)
HHHHHHSSGLGVLFQGPGSKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLIPGLPAY
ILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQY
SGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLE
HETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMSQHGMDPELIKQVVKQ
MFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAA
QLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDR
KDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFIARV
Sequence of entity 2 (C, D), FASTA
>4KP3_2 RILP-like protein 2 (chains C, D)
GPGSEFMEDHPVREEEDGEEDEGALAKSPLQLTTDDVYDISYVVGRELMALGSDPRVTRL
QFKIVRVMEMLETLVNEGSLAVEELRMERDNLKQEVEGLRKAG
Sequence of entity 3 (E, F), FASTA
>4KP3_3 Melanophilin (chains E, F)
GPGSDLDTEARDQPLNSKKKKRLLSFRDVDFEEDSDHLVQPCS
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
- 3WB8 2.5 Å, Crystal Structure of MyoVa-GTD
- 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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