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4QI1

Crystal structure of H. walsbyi bacteriorhodopsin

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
A1902600biological_processproton transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0007602biological_processphototransduction
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B1902600biological_processproton transmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0007602biological_processphototransduction
C0009881molecular_functionphotoreceptor activity
C0016020cellular_componentmembrane
C1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RET A 301
ChainResidue
ATRP94
ATHR97
ATHR98
ALEU101
ASER149
ATHR150
ATRP190
ATYR193
ALYS224

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPG A 302
ChainResidue
APHE96
ALEU103
AILE116
AALA124
AMPG304
CPHE96

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MPG A 303
ChainResidue
AMET31
AILE35
AGLY38
ALEU39
ALYS47
AILE54
AALA58
AALA61
BILE122
BPHE125
BSER152
BTYR159

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE MPG A 304
ChainResidue
AARG114
AASP115
AGLY117
AALA118
AGLY121
AALA124
AVAL128
AMPG302
CLYS47
CGLU48
CVAL51
CILE52
CLEU55
CILE59
CMPG302
CHOH482

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AGLU14
ATYR210
BVAL83

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE RET B 301
ChainResidue
BTRP94
BTHR97
BTHR98
BSER149
BTHR150
BTRP190
BTYR193
BLYS224

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MPG B 302
ChainResidue
BGLU48
BLEU55
BILE59
BALA89
BHOH447
BHOH523
BHOH595
CARG114
CGLY117
CGLY121
CALA124
CVAL128
CVAL132

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPG B 303
ChainResidue
APHE96
AHOH569
BTHR74
BTRP88
BLEU135
BLYS137
CHOH444

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPG B 304
ChainResidue
BTHR147
BPHE155
BTYR158
BTYR159

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPG B 305
ChainResidue
BLEU157
BTYR158
BVAL161
BGLU166

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MPG B 306
ChainResidue
BTHR24
BMET31
BGLY38
BLEU39
BALA61
BHOH591
CILE122
CPHE125
CTYR159

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RET C 301
ChainResidue
CLYS224
CTRP94
CTHR98
CMET126
CSER149
CTHR150
CTRP190
CTYR193
CASP220

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPG C 302
ChainResidue
AMPG304
CPHE96
CPRO99
CSER112
CGLN113
CARG114
CHOH505

Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDLvAKvGF
ChainResidueDetails
APHE216-PHE227

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL
ChainResidueDetails
AARG90-LEU102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues420
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLU16-ALA36
BTYR91-ALA111
BILE116-THR136
BALA144-PHE164
BILE185-ALA205
BGLU212-LEU232
CGLU16-ALA36
CVAL51-PHE71
CTYR91-ALA111
CILE116-THR136
CALA144-PHE164
AVAL51-PHE71
CILE185-ALA205
CGLU212-LEU232
ATYR91-ALA111
AILE116-THR136
AALA144-PHE164
AILE185-ALA205
AGLU212-LEU232
BGLU16-ALA36
BVAL51-PHE71

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Primary proton acceptor => ECO:0000250
ChainResidueDetails
AASP93
BASP93
CASP93

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000250
ChainResidueDetails
AGLN7
BGLN7
CGLN7

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000250
ChainResidueDetails
ALYS224
BLYS224
CLYS224

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PDB entries from 2024-10-30

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