3PSO: Mouse VPS29

Crystal structure of mouse VPS29 complexed with Zn2+. Determined by X-ray diffraction at 3.2 Å resolution. Released 15 Dec 2010.

Method
X-ray diffraction
Resolution
3.2 Å
Organism
Mus musculus
Chains
2
Atoms
2,916
Mol. weight
43.71 kDa
Ligands
ZN
Released
15 Dec 2010

Explore 3PSO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PSO contains 6 α-helices and 22 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.

Chains A and B: 3 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand2-651
α-helix20-234
β-strand33-3641
α-helix43-5210
β-strand55-5841
β-strand72-7762
β-strand80-8562
α-helix96-1005
β-strand110-11342
β-strand120-12342
β-strand128-13142
β-strand149-15681
β-strand159-168101
β-strand171-180101

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar protein sorting-associated protein 29A, Bprotein192Mus musculusQ9QZ88 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3PSO_1 Vacuolar protein sorting-associated protein 29 (chains A, B)
GSPEFGTRDRMLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLK
TLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDI
LISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGD
DVKVERIEYKKS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn7

Primary citation

Conformational dynamics and biomolecular interactions of VPS29 studied by NMR and X-ray crystallography. Swarbrick, J., Shaw, D., Chhabra, S. et al. To be published.

Other PDB entries of the same protein (UniProt Q9QZ88 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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