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5OSA

GLIC-GABAAR alpha1 chimera crystallized at pH4.6

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 Residues6
Detailsbinding site for residue ACT A 501
ChainResidue
AARG76
AILE130
AGLU180
EILE24
EPHE41
EARG104

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 502
ChainResidue
AARG84
AILE72
APRO73
AILE75

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
APHE77
AARG84

site_idAC4
Number of Residues1
Detailsbinding site for residue CL A 504
ChainResidue
DHOH608

site_idAC5
Number of Residues1
Detailsbinding site for residue D12 A 506
ChainResidue
ALEU394

site_idAC6
Number of Residues3
Detailsbinding site for residue Y01 A 507
ChainResidue
ASER269
AALA294
EILE227

site_idAC7
Number of Residues5
Detailsbinding site for residue ACT B 501
ChainResidue
APHE41
AARG104
BARG76
BILE130
BGLU180

site_idAC8
Number of Residues2
Detailsbinding site for residue CL B 502
ChainResidue
BPHE77
BARG84

site_idAC9
Number of Residues3
Detailsbinding site for residue Y01 B 505
ChainResidue
BSER269
BALA290
BPHE297

site_idAD1
Number of Residues5
Detailsbinding site for residue ACT C 501
ChainResidue
BPHE41
BARG104
CARG76
CILE130
CGLU180

site_idAD2
Number of Residues3
Detailsbinding site for residue ACT C 502
ChainResidue
CPRO73
CILE75
CARG84

site_idAD3
Number of Residues2
Detailsbinding site for residue CL C 503
ChainResidue
CPHE77
CARG84

site_idAD4
Number of Residues5
Detailsbinding site for residue Y01 C 505
ChainResidue
BLEU231
CSER269
CASP286
CALA290
CALA294

site_idAD5
Number of Residues5
Detailsbinding site for residue ACT D 501
ChainResidue
CPHE41
CARG104
DARG76
DILE130
DGLU180

site_idAD6
Number of Residues3
Detailsbinding site for residue ACT D 502
ChainResidue
DPRO73
DILE75
DARG84

site_idAD7
Number of Residues2
Detailsbinding site for residue CL D 503
ChainResidue
DPHE77
DARG84

site_idAD8
Number of Residues2
Detailsbinding site for residue D12 D 505
ChainResidue
DASN407
DTRP411

site_idAD9
Number of Residues4
Detailsbinding site for residue Y01 D 506
ChainResidue
DSER269
DASP286
DTYR293
DALA294

site_idAE1
Number of Residues5
Detailsbinding site for residue ACT E 501
ChainResidue
DPHE41
DARG104
EARG76
EILE130
EGLU180

site_idAE2
Number of Residues2
Detailsbinding site for residue CL E 502
ChainResidue
EPHE77
EARG84

site_idAE3
Number of Residues3
Detailsbinding site for residue D12 E 504
ChainResidue
ETYR193
ETRP411
ELEU415

site_idAE4
Number of Residues5
Detailsbinding site for residue Y01 E 505
ChainResidue
DILE227
DMET235
ESER269
EASP286
EALA294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues955
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
AGLN1-GLN192
BGLN1-GLN192
CGLN1-GLN192
DGLN1-GLN192
EGLN1-GLN192

site_idSWS_FT_FI2
Number of Residues405
DetailsTRANSMEM: Helical => ECO:0000250|UniProtKB:P14867
ChainResidueDetails
AVAL226-LEU246
CPRO252-ARG273
CALA284-THR305
CLEU394-THR413
DVAL226-LEU246
DPRO252-ARG273
DALA284-THR305
DLEU394-THR413
EVAL226-LEU246
EPRO252-ARG273
EALA284-THR305
APRO252-ARG273
ELEU394-THR413
AALA284-THR305
ALEU394-THR413
BVAL226-LEU246
BPRO252-ARG273
BALA284-THR305
BLEU394-THR413
CVAL226-LEU246

site_idSWS_FT_FI3
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AASN247-VAL251
BASN247-VAL251
CASN247-VAL251
DASN247-VAL251
EASN247-VAL251

site_idSWS_FT_FI4
Number of Residues115
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AASN274-THR283
ETYR414-GLN428
ATYR414-GLN428
BASN274-THR283
BTYR414-GLN428
CASN274-THR283
CTYR414-GLN428
DASN274-THR283
DTYR414-GLN428
EASN274-THR283

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PDB entries from 2024-07-17

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