9VVO

cryo-EM structure of gastric proton pump bound to YK01

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005215	molecular_function	transporter activity
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006813	biological_process	potassium ion transport
A	0008556	molecular_function	P-type potassium transmembrane transporter activity
A	0008900	molecular_function	P-type potassium:proton transporter activity
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0030955	molecular_function	potassium ion binding
A	0071805	biological_process	potassium ion transmembrane transport
B	0001671	molecular_function	ATPase activator activity
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0005889	cellular_component	potassium:proton exchanging ATPase complex
B	0005890	cellular_component	sodium:potassium-exchanging ATPase complex
B	0006813	biological_process	potassium ion transport
B	0006814	biological_process	sodium ion transport
B	0006883	biological_process	intracellular sodium ion homeostasis
B	0016324	cellular_component	apical plasma membrane
B	0030007	biological_process	intracellular potassium ion homeostasis
B	0036376	biological_process	sodium ion export across plasma membrane
B	0071805	biological_process	potassium ion transmembrane transport
B	1990573	biological_process	potassium ion import across plasma membrane

Functional Information from PROSITE/UniProt

site_id	PS00391
Number of Residues	16
Details	ATPASE_NA_K_BETA_2 Sodium and potassium ATPases beta subunits signature 2. KfsCKftadmLqnCSG

Chain	Residue	Details
B	LYS149-GLY164

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	232
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	96
Details	Region: {"description":"immunoglobulin-like","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"P18597","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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