Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5OSB

GLIC-GABAAR alpha1 chimera crystallized in complex with THDOC at pH4.5

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 Residues7
Detailsbinding site for residue A8Z A 501
ChainResidue
AALA304
ATHR305
ATYR308
APHE309
EGLN241
EVAL242
EPRO400

site_idAC2
Number of Residues7
Detailsbinding site for residue A8Z A 502
ChainResidue
APRO400
BALA304
BTHR305
BTYR308
BPHE309
AGLN241
AVAL242

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 503
ChainResidue
AARG76
AILE130
AGLU180
EPHE41
EARG104

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 504
ChainResidue
APHE77
AARG84

site_idAC5
Number of Residues7
Detailsbinding site for residue A8Z B 501
ChainResidue
BGLN241
BVAL242
BTRP245
BPRO400
CALA304
CTHR305
CTYR308

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT B 502
ChainResidue
APHE41
AARG104
BARG76
BILE130
BGLU180

site_idAC7
Number of Residues7
Detailsbinding site for residue A8Z C 501
ChainResidue
CGLN241
CVAL242
CPRO400
DALA304
DTHR305
DTYR308
DPHE309

site_idAC8
Number of Residues6
Detailsbinding site for residue ACT C 502
ChainResidue
BPHE41
BARG104
CARG76
CILE130
CLEU175
CGLU180

site_idAC9
Number of Residues5
Detailsbinding site for residue ACT D 501
ChainResidue
CPHE41
CARG104
DARG76
DILE130
DGLU180

site_idAD1
Number of Residues2
Detailsbinding site for residue CL D 502
ChainResidue
DPHE77
DARG84

site_idAD2
Number of Residues6
Detailsbinding site for residue A8Z E 501
ChainResidue
DGLN241
DVAL242
EALA304
ETHR305
ETYR308
EPHE309

site_idAD3
Number of Residues5
Detailsbinding site for residue ACT E 502
ChainResidue
DPHE41
DARG104
EARG76
EILE130
EGLU180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues405
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P14867","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues45
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14867","evidenceCode":"ECO:0000250"},{"source":"UniProtKB","id":"P62813","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62813","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues230
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues35
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon