2G3K: C-terminal domain of Vps28

Crystal structure of the C-terminal domain of Vps28. Determined by X-ray diffraction at 3.05 Å resolution. Released 27 Jun 2006.

Method
X-ray diffraction
Resolution
3.05 Å
Organism
Saccharomyces cerevisiae
Chains
7
Atoms
5,446
Mol. weight
76.67 kDa
Released
27 Jun 2006

Explore 2G3K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2G3K contains 30 α-helices and 12 β-strands across 7 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix150-16718
β-strand17311
α-helix174-19118
α-helix199-21012
α-helix212-2132
β-strand21711
α-helix220-24021
Chain B: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix150-16819
β-strand17312
α-helix174-18916
α-helix199-21012
β-strand21712
α-helix220-23819
Chains C and F: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix150-16819
β-strand17313
α-helix174-19118
α-helix199-21012
β-strand21713
α-helix220-23920
Chain D: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix150-16819
α-helix174-19118
α-helix199-21113
α-helix220-23920
Chain E: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix150-16819
β-strand17314
α-helix174-18916
α-helix199-21012
α-helix2131
β-strand21714
α-helix220-23920
Chain G: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix150-16718
β-strand17316
α-helix174-19118
α-helix199-21012
β-strand21716
α-helix220-23920

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar protein sorting-associated protein VPS28A, B, C, D, E, F, Gprotein94Saccharomyces cerevisiaeQ02767 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>2G3K_1 Vacuolar protein sorting-associated protein VPS28 (chains A, B, C, D, E, F, G)
FNAKYVAEATGNFITVMDALKLNYNAKDQLHPLLAELLISINRVTRDDFENRSKLIDWIV
RINKLSIGDTLTETQIRELLFDLELAYKSFYALL

Primary citation

The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Pineda-Molina, E., Belrhali, H., Piefer, A.J. et al. Traffic (2006) 7:1007-1016. DOI 10.1111/j.1600-0854.2006.00440.x · PubMed

Other PDB entries of the same protein (UniProt Q02767 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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