Lip5(mit)2. Determined by solution NMR. Released 28 Nov 2012.
Explore 2LXL in 3D Show helices and sheets RCSB PDB PDBe
2LXL contains 9 α-helices and 0 β-strands across 1 chain. 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 | 5-9 | 5 | |
| α-helix | 12-14 | 3 | |
| α-helix | 18-30 | 13 | |
| α-helix | 32-49 | 18 | |
| α-helix | 56-74 | 19 | |
| α-helix | 78-81 | 4 | |
| α-helix | 83-106 | 24 | |
| α-helix | 112-129 | 18 | |
| α-helix | 136-157 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein VTA1 homolog | A | protein | 183 | Homo sapiens | Q9NP79 (AlphaFold model) |
>2LXL_1 Vacuolar protein sorting-associated protein VTA1 homolog (chains A) MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFL SKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYT ASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVGIEEDNDIEENED AGA
Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport. Skalicky, J.J., Arii, J., Wenzel, D.M. et al. J Biol Chem (2012) 287:43910-43926. DOI 10.1074/jbc.M112.417899 · 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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