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9VDL

Cryo-EM structure of human ATP9A in BeF-bound E2P state closed form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002020molecular_functionprotease binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005770cellular_componentlate endosome
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A0006895biological_processGolgi to endosome transport
A0006897biological_processendocytosis
A0031901cellular_componentearly endosome membrane
A0031902cellular_componentlate endosome membrane
A0032588cellular_componenttrans-Golgi network membrane
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0048812biological_processneuron projection morphogenesis
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A1903542biological_processnegative regulation of exosomal secretion
A1905279biological_processregulation of retrograde transport, endosome to Golgi
A2001135biological_processregulation of endocytic recycling
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
ABFD391-THR397

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues206
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues217
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q9HD20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P40527","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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