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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
A0005768cellular_componentendosome
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
B0005768cellular_componentendosome
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 Residues382
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29872228
ChainResidueDetails
AMET1-SER107
BTHR366-SER382
BGLY447-LEU467
BSER517-SER528
AVAL156-LYS186
APRO289-SER297
ATHR366-SER382
AGLY447-LEU467
ASER517-SER528
BMET1-SER107
BVAL156-LYS186
BPRO289-SER297

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:29872228
ChainResidueDetails
AILE108-TRP128
BILE108-TRP128

site_idSWS_FT_FI3
Number of Residues220
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:29872228
ChainResidueDetails
AGLY129-GLY134
BASN489-ARG495
AASN214-HIS271
AGLN323-ARG344
APRO404-ASP425
AASN489-ARG495
BGLY129-GLY134
BASN214-HIS271
BGLN323-ARG344
BPRO404-ASP425

site_idSWS_FT_FI4
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:29872228
ChainResidueDetails
APHE135-ARG155
BPHE135-ARG155

site_idSWS_FT_FI5
Number of Residues52
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:29872228
ChainResidueDetails
ATRP187-PHE213
BTRP187-PHE213

site_idSWS_FT_FI6
Number of Residues32
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:29872228
ChainResidueDetails
ATRP272-LEU288
BTRP272-LEU288

site_idSWS_FT_FI7
Number of Residues48
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:29872228
ChainResidueDetails
APHE298-ILE322
BPHE298-ILE322

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:29872228
ChainResidueDetails
ATHR345-ILE365
BTHR345-ILE365

site_idSWS_FT_FI9
Number of Residues40
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:29872228
ChainResidueDetails
ALEU383-PHE403
BLEU383-PHE403

site_idSWS_FT_FI10
Number of Residues40
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:29872228
ChainResidueDetails
AILE426-LEU446
BILE426-LEU446

site_idSWS_FT_FI11
Number of Residues40
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:29872228
ChainResidueDetails
AHIS468-PRO488
BHIS468-PRO488

site_idSWS_FT_FI12
Number of Residues40
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:29872228
ChainResidueDetails
ATYR496-VAL516
BTYR496-VAL516

site_idSWS_FT_FI13
Number of Residues40
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:29872228
ChainResidueDetails
ATHR529-MET549
BTHR529-MET549

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29872228, ECO:0007744|PDB:6C08
ChainResidueDetails
ASER122
BSER122

site_idSWS_FT_FI15
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AGLN227
AGLN235
AGLN252
AGLN263
BGLN227
BGLN235
BGLN252
BGLN263

222415

PDB entries from 2024-07-10

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