[English] 日本語
Yorodumi
- PDB-36qw: Arabidopsis thaliana V-type ATPase, State 3, Backbone model -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 36qw
TitleArabidopsis thaliana V-type ATPase, State 3, Backbone model
Components
  • (V-type proton ATPase subunit ...) x 14
  • V-type proton ATPase catalytic subunit A
KeywordsHYDROLASE / Membrane protein / protein complex / pH regulation
Function / homology
Function and homology information


regulation of auxin polar transport / zinc ion sequestering activity / plant-type cell wall biogenesis / diphosphate hydrolysis-driven proton transmembrane transporter activity / proton-transporting two-sector ATPase complex / unidimensional cell growth / glucose mediated signaling pathway / plant-type vacuole membrane / proton-transporting V-type ATPase, V1 domain / proton-transporting two-sector ATPase complex, catalytic domain ...regulation of auxin polar transport / zinc ion sequestering activity / plant-type cell wall biogenesis / diphosphate hydrolysis-driven proton transmembrane transporter activity / proton-transporting two-sector ATPase complex / unidimensional cell growth / glucose mediated signaling pathway / plant-type vacuole membrane / proton-transporting V-type ATPase, V1 domain / proton-transporting two-sector ATPase complex, catalytic domain / lysosomal lumen acidification / pollen development / proton-transporting V-type ATPase, V0 domain / plant-type cell wall / embryo development ending in seed dormancy / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar transport / vacuolar proton-transporting V-type ATPase, V0 domain / negative regulation of actin filament depolymerization / vacuolar proton-transporting V-type ATPase complex / plasmodesma / plant-type vacuole / chloroplast envelope / vacuolar acidification / actin filament capping / vacuole / vacuolar membrane / proton motive force-driven ATP synthesis / Golgi organization / proton-transporting ATPase activity, rotational mechanism / actin filament bundle assembly / H+-transporting two-sector ATPase / ATP metabolic process / response to cold / proton-transporting ATP synthase activity, rotational mechanism / proton transmembrane transport / chloroplast / cytoplasmic stress granule / cytosolic ribosome / actin filament binding / ATPase binding / protease binding / structural constituent of ribosome / Golgi membrane / regulation of transcription by RNA polymerase II / endoplasmic reticulum membrane / Golgi apparatus / ATP hydrolysis activity / protein-containing complex / mitochondrion / extracellular region / ATP binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
: / Domain of unknown function (DUF7794) / ATPase, V1 complex, subunit H / ATPase, V1 complex, subunit H, C-terminal / ATPase, V1 complex, subunit H, C-terminal domain superfamily / V-ATPase subunit H / V-ATPase subunit H / ATPase, V1 complex, subunit A / ATPase, V1 complex, subunit C / Vacuolar ATP synthase subunit C superfamily ...: / Domain of unknown function (DUF7794) / ATPase, V1 complex, subunit H / ATPase, V1 complex, subunit H, C-terminal / ATPase, V1 complex, subunit H, C-terminal domain superfamily / V-ATPase subunit H / V-ATPase subunit H / ATPase, V1 complex, subunit A / ATPase, V1 complex, subunit C / Vacuolar ATP synthase subunit C superfamily / V-ATPase subunit C / Vacuolar (H+)-ATPase G subunit / V-type proton ATPase subunit S1/VOA1, transmembrane domain / Vacuolar (H+)-ATPase G subunit / V0 complex accessory subunit Ac45/VOA1 transmembrane domain / ATPase, V1 complex, subunit B / ATPase, V1 complex, subunit F, eukaryotic / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H / ATPase, V0 complex, subunit d / V-ATPase proteolipid subunit C, eukaryotic / ATPase, V0 complex, subunit 116kDa, eukaryotic / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d / V-type ATP synthase subunit c/d subunit superfamily / V-type ATP synthase c/d subunit, domain 3 superfamily / ATP synthase (C/AC39) subunit / V-ATPase proteolipid subunit / V-type ATPase, V0 complex, 116kDa subunit family / V-type ATPase 116kDa subunit family / V-type ATPase subunit E / V-type ATPase subunit E, C-terminal domain superfamily / ATP synthase (E/31 kDa) subunit / ATPase, V1 complex, subunit D / ATPase, V1 complex, subunit F / ATPase, V1 complex, subunit F superfamily / ATP synthase subunit D / ATP synthase (F/14-kDa) subunit / V-type ATP synthase regulatory subunit B/beta / V-type ATP synthase catalytic alpha chain / ATPsynthase alpha/beta subunit, N-terminal extension / ATPsynthase alpha/beta subunit barrel-sandwich domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / : / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / C-terminal domain of V and A type ATP synthase / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Armadillo-like helical / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit G1 / V-type proton ATPase subunit c1 / V-type proton ATPase subunit B1 / V-type proton ATPase subunit E1 / V-type proton ATPase subunit a3 / Uncharacterized protein At3g13410 / V-type proton ATPase subunit d1 / V-type proton ATPase subunit H ...ADENOSINE-5'-DIPHOSPHATE / V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit G1 / V-type proton ATPase subunit c1 / V-type proton ATPase subunit B1 / V-type proton ATPase subunit E1 / V-type proton ATPase subunit a3 / Uncharacterized protein At3g13410 / V-type proton ATPase subunit d1 / V-type proton ATPase subunit H / V-type proton ATPase subunit C / V-type proton ATPase subunit e2 / V-type proton ATPase subunit c''1 / V-type proton ATPase subunit D / V-type proton ATPase subunit F / AT3g24160/MUJ8_16
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
AuthorsKhamina, M. / Rubinstein, J.L.
Funding support Canada, Germany, 2items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)PJT195707 Canada
German Research Foundation (DFG)CRC1101 Germany
CitationJournal: To Be Published
Title: Cryo-EM structure of the Arabidopsis thaliana V-type ATPase
Authors: Khamina, M. / Wunsch, N. / Lupanga, U. / Fink, F. / Wang, H. / Schulze, W.X. / Schumacher, K. / Rubinstein, J.L.
History
DepositionJun 26, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 9, 2026Provider: repository / Type: Initial release
Revision 1.0Sep 9, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
F: V-type proton ATPase subunit B1
G: V-type proton ATPase subunit E1
H: V-type proton ATPase subunit G1
I: V-type proton ATPase subunit E1
J: V-type proton ATPase subunit G1
K: V-type proton ATPase subunit E1
L: V-type proton ATPase subunit G1
M: V-type proton ATPase subunit D
N: V-type proton ATPase subunit F
P: V-type proton ATPase subunit H
b: V-type proton ATPase subunit AP1 fragment
c: V-type proton ATPase subunit c''1
d: V-type proton ATPase subunit d1
e: V-type proton ATPase subunit e2
g: V-type proton ATPase subunit c1
h: V-type proton ATPase subunit c1
i: V-type proton ATPase subunit c1
j: V-type proton ATPase subunit c1
k: V-type proton ATPase subunit c1
l: V-type proton ATPase subunit c1
m: V-type proton ATPase subunit c1
n: V-type proton ATPase subunit c1
o: V-type proton ATPase subunit c1
r: V-type proton ATPase subunit AP2 fragment
O: V-type proton ATPase subunit C
a: V-type proton ATPase subunit a3
C: V-type proton ATPase catalytic subunit A
E: V-type proton ATPase catalytic subunit A
D: V-type proton ATPase subunit B1
B: V-type proton ATPase subunit B1
A: V-type proton ATPase catalytic subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,004,79633
Polymers1,004,34431
Non-polymers4522
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

-
Components

-
V-type proton ATPase subunit ... , 14 types, 28 molecules FDBGIKHJLMNPbcdeghijklmnorOa

#1: Protein V-type proton ATPase subunit B1 / V-ATPase subunit B1 / V-ATPase 57 kDa subunit / Vacuolar H(+)-ATPase subunit B isoform 1 / Vacuolar ...V-ATPase subunit B1 / V-ATPase 57 kDa subunit / Vacuolar H(+)-ATPase subunit B isoform 1 / Vacuolar proton pump subunit B1


Mass: 54164.352 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: P11574
#2: Protein V-type proton ATPase subunit E1 / V-ATPase subunit E1 / Protein EMBRYO DEFECTIVE 2448 / Vacuolar H(+)-ATPase subunit E isoform 1 / ...V-ATPase subunit E1 / Protein EMBRYO DEFECTIVE 2448 / Vacuolar H(+)-ATPase subunit E isoform 1 / Vacuolar proton pump subunit E1


Mass: 26101.053 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q39258
#3: Protein V-type proton ATPase subunit G1 / V-ATPase subunit G1 / Vacuolar H(+)-ATPase subunit G isoform 1 / Vacuolar proton pump subunit G1


Mass: 12416.915 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: O82628
#4: Protein V-type proton ATPase subunit D / V-ATPase subunit D / Vacuolar H(+)-ATPase subunit D / Vacuolar proton pump subunit D


Mass: 29104.756 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9XGM1
#5: Protein V-type proton ATPase subunit F / V-ATPase subunit F / V-ATPase 14 kDa subunit / Vacuolar H(+)-ATPase subunit F / Vacuolar proton pump subunit F


Mass: 14276.354 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9ZQX4
#6: Protein V-type proton ATPase subunit H / V-ATPase subunit H / Vacuolar H(+)-ATPase subunit H / Vacuolar proton pump subunit H


Mass: 50346.262 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9LX65
#7: Protein V-type proton ATPase subunit AP1 fragment


Mass: 35015.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q93WB8
#8: Protein V-type proton ATPase subunit c''1 / V-ATPase subunit c''1 / Vacuolar H(+)-ATPase subunit c'' isoform 1 / Vacuolar proton pump subunit c''1


Mass: 18383.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9SZY7
#9: Protein V-type proton ATPase subunit d1 / V-ATPase subunit d1 / Vacuolar H(+)-ATPase subunit d isoform 1 / Vacuolar proton pump subunit d1


Mass: 40835.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9LJI5
#10: Protein V-type proton ATPase subunit e2 / V-ATPase subunit e2 / Vacuolar H(+)-ATPase subunit e isoform 2 / Vacuolar proton pump subunit e2


Mass: 7688.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9SZ13
#11: Protein
V-type proton ATPase subunit c1 / V-ATPase subunit c1 / V-type proton ATPase 16 kDa proteolipid subunit c1 / V-ATPase 16 kDa ...V-ATPase subunit c1 / V-type proton ATPase 16 kDa proteolipid subunit c1 / V-ATPase 16 kDa proteolipid subunit c1 / Vacuolar H(+)-ATPase subunit c isoform 1 / Vacuolar proton pump 16 kDa proteolipid subunit c1 / Vacuolar proton pump subunit c1


Mass: 16581.588 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: P0DH92
#12: Protein V-type proton ATPase subunit AP2 fragment / Putative type 1 membrane protein / Type 1 membrane protein / putative


Mass: 39164.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9ZSJ7
#13: Protein V-type proton ATPase subunit C / V-ATPase subunit C / Vacuolar H(+)-ATPase subunit C / Vacuolar proton pump subunit C


Mass: 42667.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9SDS7
#14: Protein V-type proton ATPase subunit a3 / V-ATPase subunit a3 / V-type proton ATPase 95 kDa subunit a isoform 3 / V-ATPase 95 kDa isoform a3 ...V-ATPase subunit a3 / V-type proton ATPase 95 kDa subunit a isoform 3 / V-ATPase 95 kDa isoform a3 / Vacuolar H(+)-ATPase subunit a isoform 3 / Vacuolar proton pump subunit a3 / Vacuolar proton translocating ATPase 95 kDa subunit a isoform 3


Mass: 92928.086 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q8W4S4

-
Protein , 1 types, 3 molecules CEA

#15: Protein V-type proton ATPase catalytic subunit A / V-ATPase subunit A / V-ATPase 69 kDa subunit / Vacuolar H(+)-ATPase subunit A / Vacuolar proton ...V-ATPase subunit A / V-ATPase 69 kDa subunit / Vacuolar H(+)-ATPase subunit A / Vacuolar proton pump subunit alpha


Mass: 68884.234 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: O23654, H+-transporting two-sector ATPase

-
Non-polymers , 2 types, 2 molecules

#16: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
#17: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION

-
Details

Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: Arabidopsis V-ATPase State 1 / Type: COMPLEX / Entity ID: #2-#11 / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER/RHODIUM / Grid mesh size: 400 divisions/in. / Grid type: Homemade
VitrificationCryogen name: ETHANE

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) / Num. of real images: 7681
EM imaging opticsEnergyfilter name: TFS Selectris X / Energyfilter slit width: 10 eV

-
Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.21.1_5286model refinement
5cryoSPARCCTF correction
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 190490
3D reconstructionResolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 42172 / Symmetry type: POINT
RefinementHighest resolution: 3 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00364081
ELECTRON MICROSCOPYf_angle_d0.5786692
ELECTRON MICROSCOPYf_dihedral_angle_d12.26723779
ELECTRON MICROSCOPYf_chiral_restr0.049951
ELECTRON MICROSCOPYf_plane_restr0.00511115

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more