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6EMX

X-ray structure of the N15'C mutant of GLIC in complex with bromoform

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 Residues2
Detailsbinding site for residue CL A 401
ChainResidue
APHE78
AARG85

site_idAC2
Number of Residues3
Detailsbinding site for residue NA A 402
ChainResidue
APRO68
AILE71
AILE73

site_idAC3
Number of Residues1
Detailsbinding site for residue NA A 403
ChainResidue
DHOH503

site_idAC4
Number of Residues1
Detailsbinding site for residue MBR A 404
ChainResidue
ATHR255

site_idAC5
Number of Residues1
Detailsbinding site for residue CL B 401
ChainResidue
BPHE78

site_idAC6
Number of Residues4
Detailsbinding site for residue NA B 402
ChainResidue
BILE71
BTRP72
BILE73
BPRO68

site_idAC7
Number of Residues1
Detailsbinding site for residue MBR B 403
ChainResidue
BTHR255

site_idAC8
Number of Residues2
Detailsbinding site for residue NA C 401
ChainResidue
CPRO68
CILE71

site_idAC9
Number of Residues2
Detailsbinding site for residue MBR C 402
ChainResidue
CPRO120
CTHR255

site_idAD1
Number of Residues1
Detailsbinding site for residue CL D 401
ChainResidue
DPHE78

site_idAD2
Number of Residues2
Detailsbinding site for residue NA D 402
ChainResidue
DPRO68
DILE71

site_idAD3
Number of Residues2
Detailsbinding site for residue MBR D 403
ChainResidue
DTHR255
DILE258

site_idAD4
Number of Residues1
Detailsbinding site for residue CL E 401
ChainResidue
EPHE78

site_idAD5
Number of Residues2
Detailsbinding site for residue NA E 402
ChainResidue
EPRO68
EILE71

site_idAD6
Number of Residues4
Detailsbinding site for residue MBR E 403
ChainResidue
BHOH501
CHOH501
ESER230
EHOH502

site_idAD7
Number of Residues5
Detailsbinding site for residue MBR E 404
ChainResidue
EPRO120
ETYR197
EILE201
ETHR255
EHOH508

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues990
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
AGLN2-GLN193
EASN245-MET252
AASN245-MET252
BGLN2-GLN193
BASN245-MET252
CGLN2-GLN193
CASN245-MET252
DGLN2-GLN193
DASN245-MET252
EGLN2-GLN193

site_idSWS_FT_FI2
Number of Residues530
DetailsTRANSMEM: Helical
ChainResidueDetails
ATYR194-PHE216
CSER220-THR244
CTHR253-VAL281
CPRO285-PHE317
DTYR194-PHE216
DSER220-THR244
DTHR253-VAL281
DPRO285-PHE317
ETYR194-PHE216
ESER220-THR244
ETHR253-VAL281
ASER220-THR244
EPRO285-PHE317
ATHR253-VAL281
APRO285-PHE317
BTYR194-PHE216
BSER220-THR244
BTHR253-VAL281
BPRO285-PHE317
CTYR194-PHE216

site_idSWS_FT_FI3
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATRP217-THR219
EGLU282-GLN284
AGLU282-GLN284
BTRP217-THR219
BGLU282-GLN284
CTRP217-THR219
CGLU282-GLN284
DTRP217-THR219
DGLU282-GLN284
ETRP217-THR219

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PDB entries from 2024-10-16

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