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9UGB

Cryo-EM structure of the Pma1 with ordered N-terminal extension in the activated state

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0005215molecular_functiontransporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0008553molecular_functionP-type proton-exporting transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0032126cellular_componenteisosome
B0045121cellular_componentmembrane raft
B0046872molecular_functionmetal ion binding
B0051453biological_processregulation of intracellular pH
B0055085biological_processtransmembrane transport
B0120029biological_processproton export across plasma membrane
B1902600biological_processproton transmembrane transport
B1902906biological_processproteasome storage granule assembly
B1904263biological_processpositive regulation of TORC1 signaling
C0000166molecular_functionnucleotide binding
C0005215molecular_functiontransporter activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0008553molecular_functionP-type proton-exporting transporter activity
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0032126cellular_componenteisosome
C0045121cellular_componentmembrane raft
C0046872molecular_functionmetal ion binding
C0051453biological_processregulation of intracellular pH
C0055085biological_processtransmembrane transport
C0120029biological_processproton export across plasma membrane
C1902600biological_processproton transmembrane transport
C1902906biological_processproteasome storage granule assembly
C1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
BASP378-THR384

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues550
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"14557538","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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