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8CQD

Cryo-EM structure of hexameric proteorhodopsin A18L mutant

Functional Information from PROSITE/UniProt
site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYiDWlLTVPLLI
ChainResidueDetails
AARG95-ILE107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:34226545
ChainResidueDetails
AALA19-TYR29
CGLY88-SER90
CGLY145-MET147
CTYR209-LEU218
EALA19-TYR29
EGLY88-SER90
EGLY145-MET147
ETYR209-LEU218
FALA19-TYR29
FGLY88-SER90
FGLY145-MET147
AGLY88-SER90
FTYR209-LEU218
DALA19-TYR29
DGLY88-SER90
DGLY145-MET147
DTYR209-LEU218
AGLY145-MET147
ATYR209-LEU218
BALA19-TYR29
BGLY88-SER90
BGLY145-MET147
BTYR209-LEU218
CALA19-TYR29

site_idSWS_FT_FI2
Number of Residues1116
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:34226545
ChainResidueDetails
ATHR30-ASP53
BPRO91-THR118
BGLY122-ALA144
BALA148-ASN177
BPRO181-GLY208
BASN219-ASN249
CTHR30-ASP53
CTRP59-THR87
CPRO91-THR118
CGLY122-ALA144
CALA148-ASN177
ATRP59-THR87
CPRO181-GLY208
CASN219-ASN249
ETHR30-ASP53
ETRP59-THR87
EPRO91-THR118
EGLY122-ALA144
EALA148-ASN177
EPRO181-GLY208
EASN219-ASN249
FTHR30-ASP53
APRO91-THR118
FTRP59-THR87
FPRO91-THR118
FGLY122-ALA144
FALA148-ASN177
FPRO181-GLY208
FASN219-ASN249
DTHR30-ASP53
DTRP59-THR87
DPRO91-THR118
DGLY122-ALA144
AGLY122-ALA144
DALA148-ASN177
DPRO181-GLY208
DASN219-ASN249
AALA148-ASN177
APRO181-GLY208
AASN219-ASN249
BTHR30-ASP53
BTRP59-THR87

site_idSWS_FT_FI3
Number of Residues54
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:34226545
ChainResidueDetails
AARG54-LYS58
CASN119-ALA121
CTHR178-SER180
CALA250
EARG54-LYS58
EASN119-ALA121
ETHR178-SER180
EALA250
FARG54-LYS58
FASN119-ALA121
FTHR178-SER180
AASN119-ALA121
FALA250
DARG54-LYS58
DASN119-ALA121
DTHR178-SER180
DALA250
ATHR178-SER180
AALA250
BARG54-LYS58
BASN119-ALA121
BTHR178-SER180
BALA250
CARG54-LYS58

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Primary proton acceptor => ECO:0000255|PIRSR:PIRSR038142-1, ECO:0000305|PubMed:34226545
ChainResidueDetails
AASP98
BASP98
CASP98
EASP98
FASP98
DASP98

site_idSWS_FT_FI5
Number of Residues6
DetailsSITE: Responsible for spectral tuning => ECO:0000255|PIRSR:PIRSR038142-1
ChainResidueDetails
ALEU106
BLEU106
CLEU106
ELEU106
FLEU106
DLEU106

site_idSWS_FT_FI6
Number of Residues6
DetailsSITE: Primary proton donor => ECO:0000255|PIRSR:PIRSR038142-1, ECO:0000305|PubMed:34226545
ChainResidueDetails
AGLU109
BGLU109
CGLU109
EGLU109
FGLU109
DGLU109

site_idSWS_FT_FI7
Number of Residues6
DetailsSITE: Proton release group => ECO:0000305|PubMed:34226545
ChainResidueDetails
AGLU143
BGLU143
CGLU143
EGLU143
FGLU143
DGLU143

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:34226545, ECO:0007744|PDB:7B03
ChainResidueDetails
ALYS232
BLYS232
CLYS232
ELYS232
FLYS232
DLYS232

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PDB entries from 2024-10-30

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