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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6NJL

Architecture and subunit arrangement of native AMPA receptors

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
F0005245molecular_functionvoltage-gated calcium channel activity
F0005246molecular_functioncalcium channel regulator activity
F0005515molecular_functionprotein binding
F0005891cellular_componentvoltage-gated calcium channel complex
F0006612biological_processprotein targeting to membrane
F0006816biological_processcalcium ion transport
F0009986cellular_componentcell surface
F0016020cellular_componentmembrane
F0016247molecular_functionchannel regulator activity
F0019226biological_processtransmission of nerve impulse
F0032281cellular_componentAMPA glutamate receptor complex
F0035255molecular_functionionotropic glutamate receptor binding
F0036477cellular_componentsomatodendritic compartment
F0044300cellular_componentcerebellar mossy fiber
F0045202cellular_componentsynapse
F0051592biological_processresponse to calcium ion
F0051968biological_processpositive regulation of synaptic transmission, glutamatergic
F0060082biological_processeye blink reflex
F0070588biological_processcalcium ion transmembrane transport
F0098685cellular_componentSchaffer collateral - CA1 synapse
F0098686cellular_componenthippocampal mossy fiber to CA3 synapse
F0098839cellular_componentpostsynaptic density membrane
F0098970biological_processpostsynaptic neurotransmitter receptor diffusion trapping
F0098978cellular_componentglutamatergic synapse
F0099072biological_processregulation of postsynaptic membrane neurotransmitter receptor levels
F0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
F1904510biological_processpositive regulation of protein localization to basolateral plasma membrane
F2000311biological_processregulation of AMPA receptor activity
F2000969biological_processpositive regulation of AMPA receptor activity
H0005245molecular_functionvoltage-gated calcium channel activity
H0005246molecular_functioncalcium channel regulator activity
H0005515molecular_functionprotein binding
H0005891cellular_componentvoltage-gated calcium channel complex
H0006612biological_processprotein targeting to membrane
H0006816biological_processcalcium ion transport
H0009986cellular_componentcell surface
H0016020cellular_componentmembrane
H0016247molecular_functionchannel regulator activity
H0019226biological_processtransmission of nerve impulse
H0032281cellular_componentAMPA glutamate receptor complex
H0035255molecular_functionionotropic glutamate receptor binding
H0036477cellular_componentsomatodendritic compartment
H0044300cellular_componentcerebellar mossy fiber
H0045202cellular_componentsynapse
H0051592biological_processresponse to calcium ion
H0051968biological_processpositive regulation of synaptic transmission, glutamatergic
H0060082biological_processeye blink reflex
H0070588biological_processcalcium ion transmembrane transport
H0098685cellular_componentSchaffer collateral - CA1 synapse
H0098686cellular_componenthippocampal mossy fiber to CA3 synapse
H0098839cellular_componentpostsynaptic density membrane
H0098970biological_processpostsynaptic neurotransmitter receptor diffusion trapping
H0098978cellular_componentglutamatergic synapse
H0099072biological_processregulation of postsynaptic membrane neurotransmitter receptor levels
H0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
H1904510biological_processpositive regulation of protein localization to basolateral plasma membrane
H2000311biological_processregulation of AMPA receptor activity
H2000969biological_processpositive regulation of AMPA receptor activity
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
JTYR193-HIS199
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues30
DetailsIntramembrane: {"description":"Helical; Pore-forming","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues348
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=M4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P42262","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7877986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21639859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SAJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues80
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues30
DetailsIntramembrane: {"description":"Helical; Pore-forming"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues348
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=M4"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11086992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16483599","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CMO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues6
DetailsSite: {"description":"Interaction with the cone snail toxin Con-ikot-ikot","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsSite: {"description":"Crucial to convey clamshell closure to channel opening","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21317873","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19946266","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21317873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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