7uwb: Difference between revisions

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== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/A0A067G267_CITSI A0A067G267_CITSI]] Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.[PIRNR:PIRNR018497]
[https://www.uniprot.org/uniprot/A0A067G267_CITSI A0A067G267_CITSI] Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.[PIRNR:PIRNR018497]
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</StructureSection>
</StructureSection>

Latest revision as of 22:33, 19 October 2022

Citrus V-ATPase State 2, Highest-Resolution ClassCitrus V-ATPase State 2, Highest-Resolution Class

Structural highlights

7uwb is a 18 chain structure with sequence from Citrus limon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A067G267_CITSI Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.[PIRNR:PIRNR018497]

7uwb, resolution 3.90Å

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OCA