Crystal structure of LIP5 N-terminal domain. Determined by X-ray diffraction at 3.01 Å resolution. Released 11 Feb 2015.
Explore 4TXP in 3D Show helices and sheets RCSB PDB PDBe
4TXP contains 32 α-helices and 0 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 8-11 | 4 | |
| α-helix | 12-17 | 6 | |
| α-helix | 18-26 | 9 | |
| α-helix | 32-49 | 18 | |
| α-helix | 54-73 | 20 | |
| α-helix | 78-81 | 4 | |
| α-helix | 83-106 | 24 | |
| α-helix | 112-128 | 17 | |
| α-helix | 129-131 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-157 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| α-helix | 12-17 | 6 | |
| α-helix | 18-26 | 9 | |
| α-helix | 32-49 | 18 | |
| α-helix | 54-73 | 20 | |
| α-helix | 78-81 | 4 | |
| α-helix | 83-106 | 24 | |
| α-helix | 112-128 | 17 | |
| α-helix | 129-131 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-157 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| α-helix | 12-17 | 6 | |
| α-helix | 18-26 | 9 | |
| α-helix | 33-49 | 17 | |
| α-helix | 56-72 | 17 | |
| α-helix | 83-106 | 24 | |
| α-helix | 112-128 | 17 | |
| α-helix | 129-131 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-157 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein VTA1 homolog | A, B, C | protein | 163 | Homo sapiens | Q9NP79 (AlphaFold model) |
>4TXP_1 Vacuolar protein sorting-associated protein VTA1 homolog (chains A, B, C) SMAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKF LSKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFY TASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETP
A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5. Vild, C.J., Li, Y., Guo, E.Z. et al. J Biol Chem (2015) 290:7291-7303. DOI 10.1074/jbc.M114.616730 · PubMed
Other PDB entries of the same protein (UniProt Q9NP79 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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