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7P9U

Cryo EM structure of System XC- in complex with glutamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0006865biological_processamino acid transport
B0003333biological_processamino acid transmembrane transport
B0005515molecular_functionprotein binding
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0006865biological_processamino acid transport
B0009636biological_processresponse to toxic substance
B0009986cellular_componentcell surface
B0015179molecular_functionL-amino acid transmembrane transporter activity
B0015252molecular_functionproton channel activity
B0015327molecular_functioncystine:glutamate antiporter activity
B0015811biological_processL-cystine transport
B0015813biological_processL-glutamate transmembrane transport
B0016020cellular_componentmembrane
B0022840molecular_functionleak channel activity
B0022857molecular_functiontransmembrane transporter activity
B0031526cellular_componentbrush border membrane
B0031528cellular_componentmicrovillus membrane
B0035752biological_processlysosomal lumen pH elevation
B0043067biological_processregulation of programmed cell death
B0045177cellular_componentapical part of cell
B0055085biological_processtransmembrane transport
B0089718biological_processamino acid import across plasma membrane
B0097449cellular_componentastrocyte projection
B0110076biological_processnegative regulation of ferroptosis
B0140924biological_processL-kynurenine transmembrane transport
B0140926molecular_functionL-kynurenine transmembrane transporter activity
B1902600biological_processproton transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"source":"PubMed","id":"30867591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues80
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"15151999","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues210
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"15151999","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues78
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15151999","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsIntramembrane: {"evidences":[{"source":"PubMed","id":"15151999","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34880232","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7P9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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