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7FJP

Cryo EM structure of lysosomal ATPase

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0000421cellular_componentautophagosome membrane
B0005215molecular_functiontransporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005768cellular_componentendosome
B0005770cellular_componentlate endosome
B0005771cellular_componentmultivesicular body
B0005776cellular_componentautophagosome
B0006874biological_processintracellular calcium ion homeostasis
B0006879biological_processintracellular iron ion homeostasis
B0006882biological_processintracellular zinc ion homeostasis
B0006914biological_processautophagy
B0007041biological_processlysosomal transport
B0008270molecular_functionzinc ion binding
B0008289molecular_functionlipid binding
B0010628biological_processpositive regulation of gene expression
B0010821biological_processregulation of mitochondrion organization
B0012506cellular_componentvesicle membrane
B0015203molecular_functionpolyamine transmembrane transporter activity
B0015417molecular_functionABC-type polyamine transporter activity
B0015662molecular_functionP-type ion transporter activity
B0016020cellular_componentmembrane
B0016241biological_processregulation of macroautophagy
B0016243biological_processregulation of autophagosome size
B0016887molecular_functionATP hydrolysis activity
B0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
B0030003biological_processintracellular monoatomic cation homeostasis
B0030133cellular_componenttransport vesicle
B0030145molecular_functionmanganese ion binding
B0031410cellular_componentcytoplasmic vesicle
B0031902cellular_componentlate endosome membrane
B0031982cellular_componentvesicle
B0032585cellular_componentmultivesicular body membrane
B0033157biological_processregulation of intracellular protein transport
B0034220biological_processmonoatomic ion transmembrane transport
B0034599biological_processcellular response to oxidative stress
B0043005cellular_componentneuron projection
B0043025cellular_componentneuronal cell body
B0043202cellular_componentlysosomal lumen
B0043523biological_processregulation of neuron apoptotic process
B0046872molecular_functionmetal ion binding
B0050714biological_processpositive regulation of protein secretion
B0055088biological_processlipid homeostasis
B0061462biological_processprotein localization to lysosome
B0061909biological_processautophagosome-lysosome fusion
B0070300molecular_functionphosphatidic acid binding
B0071287biological_processcellular response to manganese ion
B0071294biological_processcellular response to zinc ion
B0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
B0097734biological_processextracellular exosome biogenesis
B0098655biological_processmonoatomic cation transmembrane transport
B0140358molecular_functionP-type transmembrane transporter activity
B1900180biological_processregulation of protein localization to nucleus
B1902047biological_processpolyamine transmembrane transport
B1903135molecular_functioncupric ion binding
B1903146biological_processregulation of autophagy of mitochondrion
B1903543biological_processpositive regulation of exosomal secretion
B1903710biological_processspermine transmembrane transport
B1904714biological_processregulation of chaperone-mediated autophagy
B1905037biological_processautophagosome organization
B1905165biological_processregulation of lysosomal protein catabolic process
B1905166biological_processnegative regulation of lysosomal protein catabolic process
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
BASP513-THR519

site_idPS01229
Number of Residues23
DetailsCOF_2 Hypothetical cof family signature 2. CGDGaNDcgaLkaAdvGisLsqA
ChainResidueDetails
BCYS876-ALA898

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues176
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues68
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"26134396","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues25
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26134396","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"PubMed","id":"26134396","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26134396","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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