2F6M: Vps23-C:Vps28-N subcomplex

Structure of a Vps23-C:Vps28-N subcomplex. Determined by X-ray diffraction at 2.1 Å resolution. Released 18 Apr 2006.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
2,913
Mol. weight
41.8 kDa
Ligands
MG, DDQ
Released
18 Apr 2006

Explore 2F6M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F6M contains 14 α-helices and 0 β-strands across 4 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix323-35129
α-helix356-38126
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix14-174
α-helix31-5828
α-helix64-8219
α-helix89-10315
α-helix109-1179
Chain C: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix323-35129
α-helix356-38025
Chain D: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix31-5828
α-helix64-8219
α-helix87-937
α-helix99-1035
α-helix109-1168

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permeaseA, Cprotein65Saccharomyces cerevisiaeP25604 (AlphaFold model)
Vacuolar protein sorting-associated protein VPS28B, Dprotein109Saccharomyces cerevisiaeQ02767 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>2F6M_1 Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease (chains A, C)
MTDGLNQLYNLVAQDYALTDTIEALSRMLHRGTIPLDTFVKQGRELARQQFLVRWHIQRI
TSPLS
Sequence of entity 2 (B, D), FASTA
>2F6M_2 Vacuolar protein sorting-associated protein VPS28 (chains B, D)
GAMDISQLFHDEVPLFDNSITSKDKEVIETLSEIYSIVITLDHVEKAYLKDSIDDTQYTN
TVDKLLKQFKVYLNSQNKEEINKHFQSIEAFADTYNITASNAITRLERG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
DDQDecylamine-n,n-dimethyl-N-oxideC12 H27 N O8

Primary citation

Structural and functional organization of the ESCRT-I trafficking complex. Kostelansky, M.S., Sun, J., Lee, S. et al. Cell (2006) 125:113-126. DOI 10.1016/j.cell.2006.01.049 · PubMed

Other PDB entries of the same protein (UniProt P25604 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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