Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6A69

Cryo-EM structure of a P-type ATPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001772cellular_componentimmunological synapse
A0001818biological_processnegative regulation of cytokine production
A0003056biological_processregulation of vascular associated smooth muscle contraction
A0005215molecular_functiontransporter activity
A0005388molecular_functionP-type calcium transporter activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0008217biological_processregulation of blood pressure
A0015085molecular_functioncalcium ion transmembrane transporter activity
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0030501biological_processpositive regulation of bone mineralization
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0034220biological_processmonoatomic ion transmembrane transport
A0042734cellular_componentpresynaptic membrane
A0042995cellular_componentcell projection
A0045202cellular_componentsynapse
A0046872molecular_functionmetal ion binding
A0051480biological_processregulation of cytosolic calcium ion concentration
A0051481biological_processnegative regulation of cytosolic calcium ion concentration
A0051928biological_processpositive regulation of calcium ion transport
A0070062cellular_componentextracellular exosome
A0070588biological_processcalcium ion transmembrane transport
A0098684cellular_componentphotoreceptor ribbon synapse
A0098978cellular_componentglutamatergic synapse
A1900076biological_processregulation of cellular response to insulin stimulus
A1903779biological_processregulation of cardiac conduction
A1990034biological_processcalcium ion export across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP475-THR481

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues159
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30190470","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues69
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q5ZWR1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q5ZWR1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues91
DetailsDomain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

PDB statisticsPDBj update infoContact PDBjnumon