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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PXD

CryoEM structure of zebra fish alpha-1 glycine receptor, Apo state

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
A0006821biological_processchloride transport
A0016020cellular_componentmembrane
A0016594molecular_functionglycine binding
A0016934molecular_functionextracellularly glycine-gated chloride channel activity
A0022824molecular_functiontransmitter-gated monoatomic ion channel activity
A0034220biological_processmonoatomic ion transmembrane transport
A0045211cellular_componentpostsynaptic membrane
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
B0006821biological_processchloride transport
B0016020cellular_componentmembrane
B0016594molecular_functionglycine binding
B0016934molecular_functionextracellularly glycine-gated chloride channel activity
B0022824molecular_functiontransmitter-gated monoatomic ion channel activity
B0034220biological_processmonoatomic ion transmembrane transport
B0045211cellular_componentpostsynaptic membrane
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
C0006821biological_processchloride transport
C0016020cellular_componentmembrane
C0016594molecular_functionglycine binding
C0016934molecular_functionextracellularly glycine-gated chloride channel activity
C0022824molecular_functiontransmitter-gated monoatomic ion channel activity
C0034220biological_processmonoatomic ion transmembrane transport
C0045211cellular_componentpostsynaptic membrane
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
D0006821biological_processchloride transport
D0016020cellular_componentmembrane
D0016594molecular_functionglycine binding
D0016934molecular_functionextracellularly glycine-gated chloride channel activity
D0022824molecular_functiontransmitter-gated monoatomic ion channel activity
D0034220biological_processmonoatomic ion transmembrane transport
D0045211cellular_componentpostsynaptic membrane
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0005886cellular_componentplasma membrane
E0006811biological_processmonoatomic ion transport
E0006821biological_processchloride transport
E0016020cellular_componentmembrane
E0016594molecular_functionglycine binding
E0016934molecular_functionextracellularly glycine-gated chloride channel activity
E0022824molecular_functiontransmitter-gated monoatomic ion channel activity
E0034220biological_processmonoatomic ion transmembrane transport
E0045211cellular_componentpostsynaptic membrane
Functional Information from PROSITE/UniProt
site_idPS00236
Number of Residues15
DetailsNEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMdLknFPmDvqtC
ChainResidueDetails
ECYS154-CYS168
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues105
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues50
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P23415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues25
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues5
DetailsSite: {"description":"Important for obstruction of the ion pore in the closed conformation","evidences":[{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26344198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-10-22

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