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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
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
A0030165molecular_functionPDZ domain binding
A0030501biological_processpositive regulation of bone mineralization
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0034220biological_processmonoatomic ion transmembrane transport
A0042734cellular_componentpresynaptic membrane
A0042995cellular_componentcell projection
A0043231cellular_componentintracellular membrane-bounded organelle
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 Residues20
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:30190470
ChainResidueDetails
BLEU224-TYR244
ASER176-LEU366
ATHR440-PHE855
ATHR904-THR927
ALYS992-ASN1005
AILE1061-SER1220

site_idSWS_FT_FI2
Number of Residues37
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BGLU245-ASN282
AGLU155-TRP175
ATHR367-ILE386
AMET928-PHE948
ATYR972-ARG991
AASN1006-GLY1027
AGLN1040-THR1060

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN55
BASN81
BASN201
AALA949-HIS971
AGLY1028-GLU1039

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN113
ALEU856-ILE876
ALYS883-ALA903

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
BASN168
BASN180

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q5ZWR1
ChainResidueDetails
AASP475
ATHR477
AASP797

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AGLY2

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER8

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER17

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:G5E829
ChainResidueDetails
ASER338

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:1827443
ChainResidueDetails
ATHR1116

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11505
ChainResidueDetails
ASER1178

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1193

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR1203

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER1216

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER1220

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PDB entries from 2024-07-17

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