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9L0D

Cryo-EM structure of the human MON1A/CCZ1/C18orf8 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0006623biological_processprotein targeting to vacuole
A0016192biological_processvesicle-mediated transport
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005765cellular_componentlysosomal membrane
B0005770cellular_componentlate endosome
B0005829cellular_componentcytosol
B0007034biological_processvacuolar transport
B0016192biological_processvesicle-mediated transport
B0035658cellular_componentMon1-Ccz1 complex
C0005085molecular_functionguanyl-nucleotide exchange factor activity
C0005515molecular_functionprotein binding
C0005765cellular_componentlysosomal membrane
C0005770cellular_componentlate endosome
C0006914biological_processautophagy
C0010506biological_processregulation of autophagy
C0031902cellular_componentlate endosome membrane
C0035658cellular_componentMon1-Ccz1 complex
D0000045biological_processautophagosome assembly
D0000166molecular_functionnucleotide binding
D0000421cellular_componentautophagosome membrane
D0003924molecular_functionGTPase activity
D0003925molecular_functionG protein activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005739cellular_componentmitochondrion
D0005764cellular_componentlysosome
D0005765cellular_componentlysosomal membrane
D0005770cellular_componentlate endosome
D0005811cellular_componentlipid droplet
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006622biological_processprotein targeting to lysosome
D0006629biological_processlipid metabolic process
D0006897biological_processendocytosis
D0006914biological_processautophagy
D0007174biological_processepidermal growth factor catabolic process
D0008333biological_processendosome to lysosome transport
D0009617biological_processresponse to bacterium
D0010008cellular_componentendosome membrane
D0015031biological_processprotein transport
D0016042biological_processlipid catabolic process
D0016787molecular_functionhydrolase activity
D0019003molecular_functionGDP binding
D0019076biological_processviral release from host cell
D0022615biological_processprotein to membrane docking
D0030667cellular_componentsecretory granule membrane
D0030670cellular_componentphagocytic vesicle membrane
D0030672cellular_componentsynaptic vesicle membrane
D0030904cellular_componentretromer complex
D0031267molecular_functionsmall GTPase binding
D0031410cellular_componentcytoplasmic vesicle
D0031902cellular_componentlate endosome membrane
D0031966cellular_componentmitochondrial membrane
D0032935molecular_functionsterol sensor activity
D0032991cellular_componentprotein-containing complex
D0033162cellular_componentmelanosome membrane
D0034045cellular_componentphagophore assembly site membrane
D0036466biological_processsynaptic vesicle recycling via endosome
D0042147biological_processretrograde transport, endosome to Golgi
D0042632biological_processcholesterol homeostasis
D0045022biological_processearly endosome to late endosome transport
D0045335cellular_componentphagocytic vesicle
D0045453biological_processbone resorption
D0045732biological_processpositive regulation of protein catabolic process
D0048524biological_processpositive regulation of viral process
D0061462biological_processprotein localization to lysosome
D0061724biological_processlipophagy
D0070062cellular_componentextracellular exosome
D0090120biological_processlysosome to ER cholesterol transport
D0090382biological_processphagosome maturation
D0090383biological_processphagosome acidification
D0090385biological_processphagosome-lysosome fusion
D0097208cellular_componentalveolar lamellar body
D0098588cellular_componentbounding membrane of organelle
D0098830cellular_componentpresynaptic endosome
D0099638biological_processendosome to plasma membrane protein transport
D1903542biological_processnegative regulation of exosomal secretion
D1903543biological_processpositive regulation of exosomal secretion
D1905366biological_processnegative regulation of intralumenal vesicle formation
D1905394molecular_functionretromer complex binding
Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VIIlGDSGVGKnsL
ChainResidueDetails
DVAL11-LEU24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues166
DetailsDomain: {"description":"Mic1"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues13
DetailsMotif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues15
DetailsMotif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by LRRK1","evidences":[{"source":"PubMed","id":"36040231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37857821","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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