6O7T: Saccharomyces cerevisiae V-ATPase Vph1-VO
Saccharomyces cerevisiae V-ATPase Vph1-VO. Determined by electron microscopy at 3.2 Å resolution. Released 3 Apr 2019.
- Method
- Electron microscopy
- Resolution
- 3.2 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 15
- Atoms
- 19,730
- Mol. weight
- 356.14 kDa
- Released
- 3 Apr 2019
Explore 6O7T in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6O7T contains 113 α-helices and 21 β-strands across 15 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: 34 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 14-19 | 6 | 1 |
| β-strand | 20-22 | 3 | 2 |
| α-helix | 29-34 | 6 | |
| β-strand | 40-41 | 2 | 1 |
| α-helix | 56-58 | 3 | |
| α-helix | 60-78 | 19 | |
| α-helix | 88-92 | 5 | |
| α-helix | 106-144 | 39 | |
| β-strand | 187-191 | 5 | 3 |
| α-helix | 196-206 | 11 | |
| β-strand | 212-217 | 6 | 3 |
| β-strand | 222 | 1 | 4 |
| β-strand | 231 | 1 | 4 |
| β-strand | 234-239 | 6 | 3 |
| α-helix | 243-255 | 13 | |
| β-strand | 261 | 1 | 3 |
| α-helix | 267-303 | 37 | |
| α-helix | 308-324 | 17 | |
| β-strand | 327-328 | 2 | 2 |
| β-strand | 334-336 | 3 | 2 |
| β-strand | 339-342 | 4 | 1 |
| α-helix | 343-345 | 3 | |
| α-helix | 346-358 | 13 | |
| β-strand | 368-370 | 3 | 1 |
| β-strand | 379 | 1 | 5 |
| α-helix | 388-391 | 4 | |
| α-helix | 404-406 | 3 | |
| α-helix | 411-423 | 13 | |
| α-helix | 426-441 | 16 | |
| α-helix | 453-460 | 8 | |
| α-helix | 463-478 | 16 | |
| β-strand | 482 | 1 | 6 |
| β-strand | 485 | 1 | 6 |
| β-strand | 494-495 | 2 | 7 |
| β-strand | 506-507 | 2 | 8 |
| β-strand | 509-510 | 2 | 7 |
| α-helix | 520-522 | 3 | |
| α-helix | 528-559 | 32 | |
| α-helix | 565-567 | 3 | |
| α-helix | 568-572 | 5 | |
| α-helix | 573-579 | 7 | |
| α-helix | 580-584 | 5 | |
| α-helix | 585-594 | 10 | |
| α-helix | 603-605 | 3 | |
| α-helix | 608-612 | 5 | |
| α-helix | 631-654 | 24 | |
| α-helix | 710-729 | 20 | |
| α-helix | 731-733 | 3 | |
| α-helix | 735-752 | 18 | |
| α-helix | 756-758 | 3 | |
| α-helix | 766-781 | 16 | |
| α-helix | 782-789 | 8 | |
| α-helix | 790-802 | 13 | |
| β-strand | 816 | 1 | 5 |
Chain b: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 221-249 | 29 | |
Chain c: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-38 | 14 | |
| α-helix | 42-44 | 3 | |
| α-helix | 47-53 | 7 | |
| α-helix | 56-88 | 33 | |
| α-helix | 94-96 | 3 | |
| α-helix | 105-122 | 18 | |
| α-helix | 136-167 | 32 | |
| α-helix | 181-205 | 25 | |
Chain d: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-20 | 10 | |
| α-helix | 28-31 | 4 | |
| α-helix | 39-46 | 8 | |
| α-helix | 65-84 | 20 | |
| α-helix | 92-114 | 23 | |
| α-helix | 120-126 | 7 | |
| α-helix | 145-151 | 7 | |
| α-helix | 177-193 | 17 | |
| α-helix | 202-227 | 26 | |
| α-helix | 252-257 | 6 | |
| α-helix | 262-268 | 7 | |
| α-helix | 288-297 | 10 | |
| α-helix | 307-331 | 25 | |
Chain e: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-23 | 19 | |
| α-helix | 30-53 | 24 | |
| β-strand | 63-64 | 2 | 8 |
Chain f: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-32 | 21 | |
| α-helix | 48-69 | 22 | |
Chain g: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-42 | 34 | |
| α-helix | 47-49 | 3 | |
| α-helix | 55-75 | 21 | |
| α-helix | 84-118 | 35 | |
| α-helix | 125-151 | 27 | |
Chain h: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-41 | 33 | |
| α-helix | 55-73 | 19 | |
| α-helix | 84-118 | 35 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-152 | 27 | |
7 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| V-type proton ATPase subunit a, vacuolar isoform | a | protein | 862 | Saccharomyces cerevisiae | P32563 (AlphaFold model) |
| V0 assembly protein 1 | b | protein | 265 | Saccharomyces cerevisiae | P53262 (AlphaFold model) |
| V-type proton ATPase subunit c'' | c | protein | 213 | Saccharomyces cerevisiae | P23968 (AlphaFold model) |
| V-type proton ATPase subunit d | d | protein | 345 | Saccharomyces cerevisiae | P32366 (AlphaFold model) |
| Putative protein YPR170W-B | f | protein | 85 | Saccharomyces cerevisiae | P0C5R9 |
| V-type proton ATPase subunit c | g, h, i, j, k, l, m, n | protein | 160 | Saccharomyces cerevisiae | P25515 |
| V-type proton ATPase subunit c' | o | protein | 164 | Saccharomyces cerevisiae | P32842 |
| V-type proton ATPase subunit e | e | protein | 73 | Saccharomyces cerevisiae | Q3E7B6 |
Sequence of entity 1 (a), FASTA
>6O7T_1 V-type proton ATPase subunit a, vacuolar isoform (chains a)
MAEKEEAIFRSAEMALVQFYIPQEISRDSAYTLGQLGLVQFRDLNSKVRAFQRTFVNEIR
RLDNVERQYRYFYSLLKKHDIKLYEGDTDKYLDGSGELYVPPSGSVIDDYVRNASYLEER
LIQMEDATDQIEVQKNDLEQYRFILQSGDEFFLKGDNTDSTSYMDEDMIDANGENIAAAI
GASVNYVTGVIARDKVATLEQILWRVLRGNLFFKTVEIEQPVYDVKTREYKHKNAFIVFS
HGDLIIKRIRKIAESLDANLYDVDSSNEGRSQQLAKVNKNLSDLYTVLKTTSTTLESELY
AIAKELDSWFQDVTREKAIFEILNKSNYDTNRKILIAEGWIPRDELATLQARLGEMIARL
GIDVPSIIQVLDTNHTPPTFHRTNKFTAGFQSICDCYGIAQYREINAGLPTIVTFPFMFA
IMFGDMGHGFLMTLAALSLVLNEKKINKMKRGEIFDMAFTGRYIILLMGVFSMYTGFLYN
DIFSKTMTIFKSGWKWPDHWKKGESITATSVGTYPIGLDWAWHGTENALLFSNSYKMKLS
ILMGFIHMTYSYFFSLANHLYFNSMIDIIGNFIPGLLFMQGIFGYLSVCIVYKWAVDWVK
DGKPAPGLLNMLINMFLSPGTIDDELYPHQAKVQVFLLLMALVCIPWLLLVKPLHFKFTH
KKKSHEPLPSTEADASSEDLEAQQLISAMDADDAEEEEVGSGSHGEDFGDIMIHQVIHTI
EFCLNCVSHTASYLRLWALSLAHAQLSSVLWTMTIQIAFGFRGFVGVFMTVALFAMWFAL
TCAVLVLMEGTSAMLHSLRLHWVESMSKFFVGEGLPYEPFAFEYKDMEVAVASASSSASS
DYKDHDGDYKDHDIDYKDDDDK
Sequence of entity 2 (b), FASTA
>6O7T_2 V0 assembly protein 1 (chains b)
MVFGQLYALFIFTLSCCISKTVQADSSKESSSFISFDKESNWDTISTISSTADVISSVDS
AIAVFEFDNFSLLDNLMIDEEYPFFNRFFANDVSLTVHDDSPLNISQSLSPIMEQFTVDE
LPESASDLLYEYSLDDKSIVLFKFTSDAYDLKKLDEFIDSCLSFLEDKSGDNLTVVINSL
GWAFEDEDGDDEYATEETLSHHDNNKGKEGDDDILSSIWTEGLLMCLIVSALLLFILIVA
LSWISNLDITYGALEKSTNPIKKNN
Sequence of entity 3 (c), FASTA
>6O7T_3 V-type proton ATPase subunit c'' (chains c)
MNKESKDDDMSLGKFSFSHFLYYLVLIVVIVYGLYKLFTGHGSDINFGKFLLRTSPYMWA
NLGIALCVGLSVVGAAWGIFITGSSMIGAGVRAPRITTKNLISIIFCEVVAIYGLIIAIV
FSSKLTVATAENMYSKSNLYTGYSLFWAGITVGASNLICGIAVGITGATAAISDAADSAL
FVKILVIEIFGSILGLLGLIVGLLMAGKASEFQ
Sequence of entity 4 (d), FASTA
>6O7T_4 V-type proton ATPase subunit d (chains d)
MEGVYFNIDNGFIEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSS
ESLTTSLIQEYASSKLYHEFNYIRDQSSGSTRKFMDYITYGYMIDNVALMITGTIHDRDK
GEILQRCHPLGWFDTLPTLSVATDLESLYETVLVDTPLAPYFKNCFDTAEELDDMNIEII
RNKLYKAYLEDFYNFVTEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSD
LLPNIGKLYPLATFHLAQAQDFEGVRAALANVYEYRGFLETGNLEDHFYQLEMELCRDAF
TQQFAISTVWAWMKSKEQEVRNITWIAECIAQNQRERINNYISVY
Sequence of entity 5 (f), FASTA
>6O7T_5 Putative protein YPR170W-B (chains f)
MRPVVSTGKAWCCTVLSAFGVVILSVIAHLFNTNHESFVGSINDPEDGPAVAHTVYLAAL
VYLVFFVFCGFQVYLARRKPSIELR
Sequence of entity 6 (g, h, i, j, k, l, m, n), FASTA
>6O7T_6 V-type proton ATPase subunit c (chains g, h, i, j, k, l, m, n)
MTELCPVYAPFFGAIGCASAIIFTSLGAAYGTAKSGVGICATCVLRPDLLFKNIVPVIMA
GIIAIYGLVVSVLVCYSLGQKQALYTGFIQLGAGLSVGLSGLAAGFAIGIVGDAGVRGSS
QQPRLFVGMILILIFAEVLGLYGLIVALLLNSRATQDVVC
Sequence of entity 7 (o), FASTA
>6O7T_7 V-type proton ATPase subunit c' (chains o)
MSTQLASNIYAPLYAPFFGFAGCAAAMVLSCLGAAIGTAKSGIGIAGIGTFKPELIMKSL
IPVVMSGILAIYGLVVAVLIAGNLSPTEDYTLFNGFMHLSCGLCVGFACLSSGYAIGMVG
DVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIVALILNTRGSE
Sequence of entity 8 (e), FASTA
>6O7T_8 V-type proton ATPase subunit e (chains e)
MSSFYTVVGVFIVVSAMSVLFWIMAPKNNQAVWRSTVILTLAMMFLMWAITFLCQLHPLV
APRRSDLRPEFAE
Primary citation
Structural comparison of the vacuolar and Golgi V-ATPases fromSaccharomyces cerevisiae. Vasanthakumar, T., Bueler, S.A., Wu, D. et al. Proc Natl Acad Sci U S A (2019) 116:7272-7277. DOI 10.1073/pnas.1814818116 · PubMed
Other PDB entries of the same protein (UniProt P32563 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8EAS 2.6 Å, Yeast VO in complex with Vma12-22p
- 6M0R 2.7 Å, 2.7A Yeast Vo state3
- 7TAP 2.8 Å, Cryo-EM structure of archazolid A bound to yeast VO V-ATPase
- 6PE4 3.1 Å, Yeast Vo motor in complex with 1 VopQ molecule
- 8EAU 3.1 Å, Yeast VO in complex with Vma21p
- 6PE5 3.2 Å, Yeast Vo motor in complex with 2 VopQ molecules
- 7TAO 3.2 Å, Cryo-EM structure of bafilomycin A1 bound to yeast VO V-ATPase
- 9E7L 3.33 Å, Yeast V-ATPase Vo proton channel bound to nanobody 2WVA7
- 9E76 3.4 Å, Yeast V-ATPase Vo proton channel bound to nanobody 1WVA25
- 6C6L 3.5 Å, Yeast Vacuolar ATPase Vo in lipid nanodisc
- 7TMR 3.5 Å, V-ATPase from Saccharomyces cerevisiae, State 1
- 6M0S 3.6 Å, 3.6A Yeast Vo state3 prime
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