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4X5T

alpha 1 glycine receptor transmembrane structure fused to the extracellular domain of GLIC

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005216molecular_functionmonoatomic ion channel activity
A0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0004888molecular_functiontransmembrane signaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0004888molecular_functiontransmembrane signaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
D0004888molecular_functiontransmembrane signaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue NI A 501
ChainResidue
AASP86
AALA87
AASP88

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 502
ChainResidue
APHE78
AARG85

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 503
ChainResidue
EARG105
AARG77
AILE131
AGLU181
EPHE42

site_idAC4
Number of Residues3
Detailsbinding site for residue NI B 501
ChainResidue
BASP86
BALA87
BASP88

site_idAC5
Number of Residues3
Detailsbinding site for residue CL B 502
ChainResidue
BPRO74
BILE76
BARG85

site_idAC6
Number of Residues2
Detailsbinding site for residue CL B 503
ChainResidue
BPHE78
BARG85

site_idAC7
Number of Residues5
Detailsbinding site for residue ACT B 504
ChainResidue
APHE42
AARG105
BARG77
BILE131
BGLU181

site_idAC8
Number of Residues3
Detailsbinding site for residue NI C 501
ChainResidue
CASP86
CALA87
CASP88

site_idAC9
Number of Residues2
Detailsbinding site for residue CL C 502
ChainResidue
CPHE78
CARG85

site_idAD1
Number of Residues3
Detailsbinding site for residue CL C 503
ChainResidue
CPRO74
CILE76
CARG85

site_idAD2
Number of Residues5
Detailsbinding site for residue ACT C 504
ChainResidue
BPHE42
BARG105
CARG77
CILE131
CGLU181

site_idAD3
Number of Residues2
Detailsbinding site for residue NI D 501
ChainResidue
DPRO74
DARG85

site_idAD4
Number of Residues3
Detailsbinding site for residue NI D 502
ChainResidue
DASP86
DALA87
DASP88

site_idAD5
Number of Residues5
Detailsbinding site for residue ACT D 503
ChainResidue
CPHE42
CARG105
DARG77
DILE131
DGLU181

site_idAD6
Number of Residues3
Detailsbinding site for residue NI E 501
ChainResidue
EASP86
EALA87
EASP88

site_idAD7
Number of Residues2
Detailsbinding site for residue CL E 502
ChainResidue
EPHE78
EARG85

site_idAD8
Number of Residues5
Detailsbinding site for residue ACT E 503
ChainResidue
DPHE42
DARG105
EARG77
EILE131
EGLU181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37821459","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8DN5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16144831","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues228
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues35
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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