4IX9: Subunit F of V-ATPase from S. cerevisiae

Crystal structure of subunit F of V-ATPase from S. cerevisiae. Determined by X-ray diffraction at 2.33 Å resolution. Released 20 Mar 2013.

Method
X-ray diffraction
Resolution
2.33 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
3,358
Mol. weight
43.99 kDa
Released
20 Mar 2013

Explore 4IX9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4IX9 contains 24 α-helices and 18 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: 6 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand7-1371
α-helix14-229
α-helix27-293
β-strand37-4041
α-helix47-559
α-helix56-605
β-strand64-6961
α-helix71-766
α-helix78-836
β-strand8612
β-strand90-9341
Chain B: 6 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand7-1263
α-helix14-229
α-helix27-293
β-strand37-3933
α-helix47-559
α-helix56-605
β-strand64-6963
α-helix71-766
α-helix78-836
β-strand90-9343
Chain C: 6 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand7-1374
α-helix14-229
α-helix27-293
β-strand37-4044
α-helix47-559
α-helix56-605
β-strand64-6964
α-helix71-766
α-helix78-825
β-strand90-9344
Chain D: 6 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand7-1265
α-helix14-229
α-helix27-293
β-strand37-3935
α-helix47-559
α-helix56-605
β-strand64-6965
α-helix71-755
α-helix78-825
β-strand8612
β-strand90-9345

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
V-type proton ATPase subunit FA, B, C, Dprotein94Saccharomyces cerevisiaeP39111 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4IX9_1 V-type proton ATPase subunit F (chains A, B, C, D)
MAEKRTLIAVIADEDTTTGLLLAGIGQITPETQEKNFFVYQEGKTTKEEITDKFNHFTEE
RDDIAILLMNQHIAENIRARVDSFTNAFPAILEI

Primary citation

Crystal and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae. Basak, S., Lim, J., Manimekalai, M.S.S. et al. J Biol Chem (2013) 288:11930-11939. DOI 10.1074/jbc.M113.461533 · PubMed

Other PDB entries of the same protein (UniProt P39111 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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