2LXM: Lip5-chmp5

Lip5-chmp5. Determined by solution NMR. Released 28 Nov 2012.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,584
Mol. weight
25.51 kDa
Released
28 Nov 2012

Explore 2LXM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-86
α-helix12-143
α-helix15-3016
α-helix32-4918
α-helix54-7421
α-helix78-814
α-helix83-10725
α-helix112-12918
α-helix136-15823
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix160-17617
α-helix181-1888

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar protein sorting-associated protein VTA1 homologAprotein168Homo sapiensQ9NP79 (AlphaFold model)
Charged multivesicular body protein 5Bprotein59Homo sapiensQ9NZZ3 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LXM_1 Vacuolar protein sorting-associated protein VTA1 homolog (chains A)
MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFL
SKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYT
ASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVG
Sequence of entity 2 (B), FASTA
>2LXM_2 Charged multivesicular body protein 5 (chains B)
GHMEDANEIQEALSRSYGTPELDEDDLEAELDALGDELLADEDSSYLDEAASAPAIPEG

Primary citation

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:

Browse structure collections

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