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7KGV

Crystal structure of sodium-coupled neutral amino acid transporter SLC38A9 in the N-terminal plugged form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003333biological_processamino acid transmembrane transport
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005770cellular_componentlate endosome
A0006110biological_processregulation of glycolytic process
A0006111biological_processregulation of gluconeogenesis
A0006520biological_processamino acid metabolic process
A0006865biological_processamino acid transport
A0006867biological_processasparagine transport
A0006868biological_processglutamine transport
A0015171molecular_functionamino acid transmembrane transporter activity
A0015179molecular_functionL-amino acid transmembrane transporter activity
A0015182molecular_functionL-asparagine transmembrane transporter activity
A0015186molecular_functionL-glutamine transmembrane transporter activity
A0015190molecular_functionL-leucine transmembrane transporter activity
A0015485molecular_functioncholesterol binding
A0015820biological_processL-leucine transport
A0016020cellular_componentmembrane
A0031902cellular_componentlate endosome membrane
A0032008biological_processpositive regulation of TOR signaling
A0032935molecular_functionsterol sensor activity
A0034618molecular_functionarginine binding
A0046872molecular_functionmetal ion binding
A0061459molecular_functionL-arginine transmembrane transporter activity
A0071230biological_processcellular response to amino acid stimulus
A0071986cellular_componentRagulator complex
A0140785molecular_functionamino acid sensor activity
A1900037biological_processregulation of cellular response to hypoxia
A1903826biological_processL-arginine transmembrane transport
A1904263biological_processpositive regulation of TORC1 signaling
B0003333biological_processamino acid transmembrane transport
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005770cellular_componentlate endosome
B0006110biological_processregulation of glycolytic process
B0006111biological_processregulation of gluconeogenesis
B0006520biological_processamino acid metabolic process
B0006865biological_processamino acid transport
B0006867biological_processasparagine transport
B0006868biological_processglutamine transport
B0015171molecular_functionamino acid transmembrane transporter activity
B0015179molecular_functionL-amino acid transmembrane transporter activity
B0015182molecular_functionL-asparagine transmembrane transporter activity
B0015186molecular_functionL-glutamine transmembrane transporter activity
B0015190molecular_functionL-leucine transmembrane transporter activity
B0015485molecular_functioncholesterol binding
B0015820biological_processL-leucine transport
B0016020cellular_componentmembrane
B0031902cellular_componentlate endosome membrane
B0032008biological_processpositive regulation of TOR signaling
B0032935molecular_functionsterol sensor activity
B0034618molecular_functionarginine binding
B0046872molecular_functionmetal ion binding
B0061459molecular_functionL-arginine transmembrane transporter activity
B0071230biological_processcellular response to amino acid stimulus
B0071986cellular_componentRagulator complex
B0140785molecular_functionamino acid sensor activity
B1900037biological_processregulation of cellular response to hypoxia
B1903826biological_processL-arginine transmembrane transport
B1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
ETYR195-HIS201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues106
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues10
DetailsRegion: {"description":"Important for arginine binding and amino acid transport","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsMotif: {"description":"CARC motif","evidences":[{"source":"UniProtKB","id":"Q8NBW4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues12
DetailsMotif: {"description":"CRAC motif","evidences":[{"source":"UniProtKB","id":"Q8NBW4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C08","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues16
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29872228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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