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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8DN2

Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state 2(expanded open)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005216molecular_functionmonoatomic ion channel activity
A0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0016594molecular_functionglycine binding
A0022824molecular_functiontransmitter-gated monoatomic ion channel activity
A0034220biological_processmonoatomic ion transmembrane transport
B0004888molecular_functiontransmembrane signaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0016594molecular_functionglycine binding
B0022824molecular_functiontransmitter-gated monoatomic ion channel activity
B0034220biological_processmonoatomic ion transmembrane transport
C0004888molecular_functiontransmembrane signaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0016594molecular_functionglycine binding
C0022824molecular_functiontransmitter-gated monoatomic ion channel activity
C0034220biological_processmonoatomic ion transmembrane transport
D0004888molecular_functiontransmembrane signaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0016594molecular_functionglycine binding
D0022824molecular_functiontransmitter-gated monoatomic ion channel activity
D0034220biological_processmonoatomic ion transmembrane transport
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0006091biological_processgeneration of precursor metabolites and energy
E0006811biological_processmonoatomic ion transport
E0008218biological_processbioluminescence
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00236
Number of Residues15
DetailsNEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMdLknFPmDvqtC
ChainResidueDetails
DCYS138-CYS152
ECYS161-CYS175
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues40
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37821459","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8DN5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16144831","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O93430","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsSite: {"description":"Important for obstruction of the ion pore in the closed conformation","evidences":[{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues11
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37821459","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DN5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BKF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsSite: {"description":"Important for obstruction of the ion pore in the closed conformation","evidences":[{"source":"UniProtKB","id":"P23415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"34473954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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