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9NRA

The structure of GluA1/A4 LBD-TMD with 4 auxiliary subunits

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
A0038023molecular_functionsignaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
B0038023molecular_functionsignaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0015276molecular_functionligand-gated monoatomic ion channel activity
C0016020cellular_componentmembrane
C0038023molecular_functionsignaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0015276molecular_functionligand-gated monoatomic ion channel activity
D0016020cellular_componentmembrane
D0038023molecular_functionsignaling receptor activity
F0006816biological_processcalcium ion transport
F0016020cellular_componentmembrane
H0006816biological_processcalcium ion transport
H0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues60
DetailsIntramembrane: {"description":"Helical; Pore-forming","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsIntramembrane: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues696
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=M4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P42262","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7877986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19022251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19102704","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20107073","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EPE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KEI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"P42262","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-05-06

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