Lip5-chmp5. Determined by solution NMR. Released 28 Nov 2012.
Explore 2LXM in 3D Show helices and sheets RCSB PDB PDBe
2LXM contains 11 α-helices and 0 β-strands across 2 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 | 3-8 | 6 | |
| α-helix | 12-14 | 3 | |
| α-helix | 15-30 | 16 | |
| α-helix | 32-49 | 18 | |
| α-helix | 54-74 | 21 | |
| α-helix | 78-81 | 4 | |
| α-helix | 83-107 | 25 | |
| α-helix | 112-129 | 18 | |
| α-helix | 136-158 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 160-176 | 17 | |
| α-helix | 181-188 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein VTA1 homolog | A | protein | 168 | Homo sapiens | Q9NP79 (AlphaFold model) |
| Charged multivesicular body protein 5 | B | protein | 59 | Homo sapiens | Q9NZZ3 (AlphaFold model) |
>2LXM_1 Vacuolar protein sorting-associated protein VTA1 homolog (chains A) MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFL SKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYT ASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVG
>2LXM_2 Charged multivesicular body protein 5 (chains B) GHMEDANEIQEALSRSYGTPELDEDDLEAELDALGDELLADEDSSYLDEAASAPAIPEG
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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