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8QRS

ASCT2 protomer in lipid nanodiscs with bound glutamine and Na+ ions in the intermediate outward-facing state (iOFS-up)

Functional Information from GO Data
ChainGOidnamespacecontents
B0001618molecular_functionvirus receptor activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006865biological_processamino acid transport
B0006868biological_processglutamine transport
B0009925cellular_componentbasal plasma membrane
B0010585biological_processglutamine secretion
B0015171molecular_functionamino acid transmembrane transporter activity
B0015175molecular_functionneutral L-amino acid transmembrane transporter activity
B0015183molecular_functionL-aspartate transmembrane transporter activity
B0015186molecular_functionL-glutamine transmembrane transporter activity
B0015194molecular_functionL-serine transmembrane transporter activity
B0015293molecular_functionsymporter activity
B0015297molecular_functionantiporter activity
B0015804biological_processneutral amino acid transport
B0015825biological_processL-serine transport
B0016020cellular_componentmembrane
B0022834molecular_functionligand-gated channel activity
B0030218biological_processerythrocyte differentiation
B0034451cellular_componentcentriolar satellite
B0036064cellular_componentciliary basal body
B0038023molecular_functionsignaling receptor activity
B0042470cellular_componentmelanosome
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0070207biological_processprotein homotrimerization
B0140009biological_processL-aspartate import across plasma membrane
B0150104biological_processtransport across blood-brain barrier
B1903803biological_processL-glutamine import across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00713
Number of Residues15
DetailsNA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. P.GElLLrLLRMIIlP
ChainResidueDetails
BPRO92-PRO106

site_idPS00714
Number of Residues24
DetailsNA_DICARBOXYL_SYMP_2 Sodium:dicarboxylate symporter family signature 2. PiGaTvNMDGAaLFqcVaaVFIAQ
ChainResidueDetails
BPRO380-GLN403

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues141
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
BMET1-ALA51
BALA117-TRP130
BGLY249-ARG257
BTHR329-PRO333
BGLU365-HIS373
BGLN483-MET541

site_idSWS_FT_FI2
Number of Residues29
DetailsTRANSMEM: Helical; Name=1 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BASN52-LEU81

site_idSWS_FT_FI3
Number of Residues126
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BGLY82-GLU94
BGLN154-GLN224
BALA286-ILE306
BILE401-LYS413
BLEU448-ASP460

site_idSWS_FT_FI4
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BLEU95-ALA116

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BALA131-LEU153

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BGLU225-LEU248

site_idSWS_FT_FI7
Number of Residues27
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BPHE258-VAL285

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BLEU307-PHE328

site_idSWS_FT_FI9
Number of Residues63
DetailsINTRAMEM: Discontinuously helical => ECO:0000305|PubMed:29872227
ChainResidueDetails
BTYR334-VAL364
BILE414-ASN447

site_idSWS_FT_FI10
Number of Residues26
DetailsTRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BILE374-PHE400

site_idSWS_FT_FI11
Number of Residues21
DetailsTRANSMEM: Helical; Name=8 => ECO:0000305|PubMed:29872227
ChainResidueDetails
BTRP461-LEU482

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O59010
ChainResidueDetails
BGLY382
BASN386
BASN471
BASP475

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P43003
ChainResidueDetails
BTHR384

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER493

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR494

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BSER503

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER535

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER539

site_idSWS_FT_FI20
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN163

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN212

237423

PDB entries from 2025-06-11

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