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7PY4

Cryo-EM structure of ATP8B1-CDC50A in E2P autoinhibited state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005319molecular_functionlipid transporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006855biological_processxenobiotic transmembrane transport
A0006869biological_processlipid transport
A0007030biological_processGolgi organization
A0007605biological_processsensory perception of sound
A0008206biological_processbile acid metabolic process
A0012505cellular_componentendomembrane system
A0015247molecular_functionaminophospholipid flippase activity
A0015711biological_processorganic anion transport
A0015721biological_processbile acid and bile salt transport
A0015914biological_processphospholipid transport
A0015917biological_processaminophospholipid transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016604cellular_componentnuclear body
A0016887molecular_functionATP hydrolysis activity
A0021650biological_processvestibulocochlear nerve formation
A0032420cellular_componentstereocilium
A0032534biological_processregulation of microvillus assembly
A0034220biological_processmonoatomic ion transmembrane transport
A0042995cellular_componentcell projection
A0045176biological_processapical protein localization
A0045332biological_processphospholipid translocation
A0045892biological_processnegative regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0060119biological_processinner ear receptor cell development
A0090554molecular_functionphosphatidylcholine floppase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140331biological_processaminophospholipid translocation
A0140345molecular_functionphosphatidylcholine flippase activity
A0140346molecular_functionphosphatidylserine flippase activity
A1901612molecular_functioncardiolipin binding
A1903729biological_processregulation of plasma membrane organization
A1990531cellular_componentphospholipid-translocating ATPase complex
A2001225biological_processregulation of chloride transport
B0005198molecular_functionstructural molecule activity
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0006855biological_processxenobiotic transmembrane transport
B0006869biological_processlipid transport
B0010976biological_processpositive regulation of neuron projection development
B0015247molecular_functionaminophospholipid flippase activity
B0015917biological_processaminophospholipid transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0030658cellular_componenttransport vesicle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031901cellular_componentearly endosome membrane
B0031902cellular_componentlate endosome membrane
B0035577cellular_componentazurophil granule membrane
B0035579cellular_componentspecific granule membrane
B0036010biological_processprotein localization to endosome
B0045332biological_processphospholipid translocation
B0061092biological_processpositive regulation of phospholipid translocation
B0070863biological_processpositive regulation of protein exit from endoplasmic reticulum
B0140331biological_processaminophospholipid translocation
B1990531cellular_componentphospholipid-translocating ATPase complex
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP454-THR460

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL50-VAL70
BGLY326-ILE346
AARG412-LYS949
ALEU1003-ARG1032
ATHR1092-PHE1097
AARG1164-SER1251

site_idSWS_FT_FI2
Number of Residues254
DetailsTOPO_DOM: Exoplasmic loop => ECO:0000255
ChainResidueDetails
BTHR71-LEU325
AALA1139-ILE1163
ASER137-ALA156
AVAL341-TRP362
ATRP390-ILE411
APHE950-PHE970
ATRP983-LEU1002
APHE1033-ALA1054
ATYR1069-ASP1091
AVAL1098-HIS1118

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M
ChainResidueDetails
BASN107
AGLU363-PHE389
APHE971-ASP982
ATYR1055-ASP1068
ASER1119-ASN1138

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M
ChainResidueDetails
BASN180

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN190
ALYS455
ATHR456
APHE596
AASN896

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M
ChainResidueDetails
BASN294
ALYS619
AARG652
ATHR732
AGLY733
AASP734
AARG867
ALYS873

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8NB49
ChainResidueDetails
AASP893
AASP897

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q148W0
ChainResidueDetails
ASER1223

226707

PDB entries from 2024-10-30

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