Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7D91

Crystal Structure of the Na+,K+-ATPase in the E2P state with bound Mg2+ (P4(3)2(1)2 symmetry)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002028	biological_process	regulation of sodium ion transport
A	0005215	molecular_function	transporter activity
A	0005391	molecular_function	P-type sodium:potassium-exchanging transporter activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005765	cellular_component	lysosomal membrane
A	0005886	cellular_component	plasma membrane
A	0005890	cellular_component	sodium:potassium-exchanging ATPase complex
A	0006813	biological_process	potassium ion transport
A	0006883	biological_process	intracellular sodium ion homeostasis
A	0008556	molecular_function	P-type potassium transmembrane transporter activity
A	0010248	biological_process	establishment or maintenance of transmembrane electrochemical gradient
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0030007	biological_process	intracellular potassium ion homeostasis
A	0030424	cellular_component	axon
A	0030955	molecular_function	potassium ion binding
A	0031402	molecular_function	sodium ion binding
A	0036376	biological_process	sodium ion export across plasma membrane
A	0042383	cellular_component	sarcolemma
A	0042470	cellular_component	melanosome
A	0051117	molecular_function	ATPase binding
A	0055085	biological_process	transmembrane transport
A	0071805	biological_process	potassium ion transmembrane transport
A	0086009	biological_process	membrane repolarization
A	1902600	biological_process	proton transmembrane transport
A	1990573	biological_process	potassium ion import across plasma membrane
B	0001671	molecular_function	ATPase activator activity
B	0005391	molecular_function	P-type sodium:potassium-exchanging transporter activity
B	0005515	molecular_function	protein binding
B	0005765	cellular_component	lysosomal membrane
B	0005886	cellular_component	plasma membrane
B	0005890	cellular_component	sodium:potassium-exchanging ATPase complex
B	0006813	biological_process	potassium ion transport
B	0006814	biological_process	sodium ion transport
B	0006874	biological_process	intracellular calcium ion homeostasis
B	0006883	biological_process	intracellular sodium ion homeostasis
B	0010248	biological_process	establishment or maintenance of transmembrane electrochemical gradient
B	0010468	biological_process	regulation of gene expression
B	0010882	biological_process	regulation of cardiac muscle contraction by calcium ion signaling
B	0014704	cellular_component	intercalated disc
B	0016020	cellular_component	membrane
B	0016323	cellular_component	basolateral plasma membrane
B	0016324	cellular_component	apical plasma membrane
B	0016328	cellular_component	lateral plasma membrane
B	0019901	molecular_function	protein kinase binding
B	0030007	biological_process	intracellular potassium ion homeostasis
B	0030315	cellular_component	T-tubule
B	0030674	molecular_function	protein-macromolecule adaptor activity
B	0035725	biological_process	sodium ion transmembrane transport
B	0036126	cellular_component	sperm flagellum
B	0036376	biological_process	sodium ion export across plasma membrane
B	0042383	cellular_component	sarcolemma
B	0046034	biological_process	ATP metabolic process
B	0050821	biological_process	protein stabilization
B	0051117	molecular_function	ATPase binding
B	0055085	biological_process	transmembrane transport
B	0055119	biological_process	relaxation of cardiac muscle
B	0060048	biological_process	cardiac muscle contraction
B	0072659	biological_process	protein localization to plasma membrane
B	0086009	biological_process	membrane repolarization
B	0141109	molecular_function	transporter activator activity
B	1901381	biological_process	positive regulation of potassium ion transmembrane transport
B	1902307	biological_process	positive regulation of sodium ion transmembrane transport
B	1902600	biological_process	proton transmembrane transport
B	1903169	biological_process	regulation of calcium ion transmembrane transport
B	1903278	biological_process	positive regulation of sodium ion export across plasma membrane
B	1903288	biological_process	positive regulation of potassium ion import across plasma membrane
B	1990573	biological_process	potassium ion import across plasma membrane
G	0001671	molecular_function	ATPase activator activity
G	0005515	molecular_function	protein binding
G	0005890	cellular_component	sodium:potassium-exchanging ATPase complex
G	0006811	biological_process	monoatomic ion transport
G	0006883	biological_process	intracellular sodium ion homeostasis
G	0010248	biological_process	establishment or maintenance of transmembrane electrochemical gradient
G	0016020	cellular_component	membrane
G	0030007	biological_process	intracellular potassium ion homeostasis
G	0030674	molecular_function	protein-macromolecule adaptor activity
G	0036376	biological_process	sodium ion export across plasma membrane
G	0043269	biological_process	regulation of monoatomic ion transport
G	0055085	biological_process	transmembrane transport
G	0099106	molecular_function	ion channel regulator activity
G	1902600	biological_process	proton transmembrane transport
G	1990573	biological_process	potassium ion import across plasma membrane

Functional Information from PROSITE/UniProt

site_id	PS00154
Number of Residues	7
Details	ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT

Chain	Residue	Details
A	BFD369-THR375

site_id	PS00390
Number of Residues	21
Details	ATPASE_NA_K_BETA_1 Sodium and potassium ATPases beta subunits signature 1. WkkFiWNsekkefLGRTggsW

Chain	Residue	Details
B	TRP12-TRP32

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

Chain	Residue	Details
B	ARG146-GLY161

site_id	PS01310
Number of Residues	14
Details	FXYD FXYD family signature. DpFyYDyeTVRngG

Chain	Residue	Details
G	ASP17-GLY30

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	212
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35380894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	81
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	174
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Region: {"description":"Phosphoinositide-3 kinase binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	19
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	121
Details	Region: {"description":"Mediates interaction with SCN7A","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	11
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P19156","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P05023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18075585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35380894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3B8E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KDP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7WYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"201","lastPage":"206","volume":"502","journal":"Nature","title":"Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state.","authors":["Kanai R.","Ogawa H.","Vilsen B.","Cornelius F.","Toyoshima C."]}},{"source":"PDB","id":"3WGU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WGV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"201","lastPage":"206","volume":"502","journal":"Nature","title":"Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state.","authors":["Kanai R.","Ogawa H.","Vilsen B.","Cornelius F.","Toyoshima C."]}},{"source":"PDB","id":"3WGV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"201","lastPage":"206","volume":"502","journal":"Nature","title":"Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state.","authors":["Kanai R.","Ogawa H.","Vilsen B.","Cornelius F.","Toyoshima C."]}},{"source":"PDB","id":"3WGU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35380894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"P05023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06685","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P06685","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	27
Details	Transmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	240
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	112
Details	Region: {"description":"immunoglobulin-like","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14094","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)