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9VVO

cryo-EM structure of gastric proton pump bound to YK01

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008900molecular_functionP-type potassium:proton transporter activity
A0016324cellular_componentapical plasma membrane
A0030955molecular_functionpotassium ion binding
A0071805biological_processpotassium ion transmembrane transport
A0090533cellular_componentcation-transporting ATPase complex
A0098797cellular_componentplasma membrane protein complex
B0001671molecular_functionATPase activator activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0005889cellular_componentpotassium:proton exchanging ATPase complex
B0005890cellular_componentsodium:potassium-exchanging ATPase complex
B0006883biological_processintracellular sodium ion homeostasis
B0016324cellular_componentapical plasma membrane
B0030007biological_processintracellular potassium ion homeostasis
B0036376biological_processsodium ion export across plasma membrane
B0071805biological_processpotassium ion transmembrane transport
B1990573biological_processpotassium ion import across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
ABFD385-THR391

site_idPS00391
Number of Residues16
DetailsATPASE_NA_K_BETA_2 Sodium and potassium ATPases beta subunits signature 2. KfsCKftadmLqnCSG
ChainResidueDetails
BLYS149-GLY164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues232
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues96
DetailsRegion: {"description":"immunoglobulin-like","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"P18597","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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