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3QBK

Bromide-bound form of pharaonis halorhodopsin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0007602biological_processphototransduction
A0009881molecular_functionphotoreceptor activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0007602biological_processphototransduction
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0007602biological_processphototransduction
D0009881molecular_functionphotoreceptor activity
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RET A 292
ChainResidue
ATRP127
ATHR131
AGLY163
ATYR180
ASER183
ATRP222
ATYR225
AASP252
ALYS256

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 22B A 300
ChainResidue
AILE49
ATHR56
ALYS65
AILE72
DTHR151
DPHE155
DALA185
DVAL189
DILE193
DGLU197

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 401
ChainResidue
ATHR126
ASER130
ALYS256

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 402
ChainResidue
AASN145
BLYS65

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 293
ChainResidue
DASN145

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE RET B 292
ChainResidue
BTRP127
BTHR131
BTYR180
BSER183
BTRP222
BTYR225
BPRO226
BLYS256

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 22B B 300
ChainResidue
APHE155
AVAL189
AILE193
AGLU197
BILE49
BVAL53
BTHR56
BLYS65
BILE72

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 401
ChainResidue
BTHR126
BSER130
BLYS256

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RET D 292
ChainResidue
DTRP127
DMET159
DTYR180
DSER183
DTRP222
DTYR225
DPRO226
DTRP229
DASP252
DLYS256

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR D 402
ChainResidue
BASN145
DLYS65

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR D 401
ChainResidue
DTHR126
DSER130
DLYS256

Functional Information from PROSITE/UniProt
site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYlTWaLSTPMIL
ChainResidueDetails
AARG123-LEU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues216
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
AMET1-ASN30
DSER87-MET120
DTHR170-SER172
DGLY232-PRO240
ASER87-MET120
ATHR170-SER172
AGLY232-PRO240
BMET1-ASN30
BSER87-MET120
BTHR170-SER172
BGLY232-PRO240
DMET1-ASN30

site_idSWS_FT_FI2
Number of Residues75
DetailsTRANSMEM: Helical; Name=Helix A => ECO:0000250
ChainResidueDetails
AASP31-THR56
BASP31-THR56
DASP31-THR56

site_idSWS_FT_FI3
Number of Residues117
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
AARG57-PRO62
DGLY143-ASN145
DVAL196-THR207
DASN270-ASP291
AGLY143-ASN145
AVAL196-THR207
AASN270-ASP291
BARG57-PRO62
BGLY143-ASN145
BVAL196-THR207
BASN270-ASP291
DARG57-PRO62

site_idSWS_FT_FI4
Number of Residues69
DetailsTRANSMEM: Helical; Name=Helix B => ECO:0000250
ChainResidueDetails
AARG63-ALA86
BARG63-ALA86
DARG63-ALA86

site_idSWS_FT_FI5
Number of Residues63
DetailsTRANSMEM: Helical; Name=Helix C => ECO:0000250
ChainResidueDetails
ATRP121-ALA142
BTRP121-ALA142
DTRP121-ALA142

site_idSWS_FT_FI6
Number of Residues69
DetailsTRANSMEM: Helical; Name=Helix D => ECO:0000250
ChainResidueDetails
AALA146-THR169
BALA146-THR169
DALA146-THR169

site_idSWS_FT_FI7
Number of Residues66
DetailsTRANSMEM: Helical; Name=Helix E => ECO:0000250
ChainResidueDetails
AHIS173-LEU195
BHIS173-LEU195
DHIS173-LEU195

site_idSWS_FT_FI8
Number of Residues69
DetailsTRANSMEM: Helical; Name=Helix F => ECO:0000250
ChainResidueDetails
AALA208-LEU231
BALA208-LEU231
DALA208-LEU231

site_idSWS_FT_FI9
Number of Residues84
DetailsTRANSMEM: Helical; Name=Helix G => ECO:0000250
ChainResidueDetails
AVAL241-SER269
BVAL241-SER269
DVAL241-SER269

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000250
ChainResidueDetails
ALYS256
BLYS256
DLYS256

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PDB entries from 2025-06-18

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