eF-site ID 4qid-AB PDB Code 4qid Chain A, B click to enlarge Title Crystal structure of Haloquadratum walsbyi bacteriorhodopsin Classification MEMBRANE PROTEIN Compound Bacteriorhodopsin-I Source Haloquadratum walsbyi (strain DSM 16790 / HBSQ001) (BACR1_HALWD) Sequence A:  GVEGEGIWLALGTIGMLLGMLYFIADGLDVQDPRQKEFYV ITILIPAIAAASYLSMFFGFGLTEVSLANGRVVDVYWARY ADWLFTTPLLLLDIGLLAGASQRDIGALVGIDAFMIVTGL VATLTKVVVARYAFWTISTISMVFLLYYLVAVFGEAVSDA DEDTRSTFNALRNIILVTWAIYPVAWLVGTEGLALTGLYG ETLLFMVLDLVAKVGFGFILLRSRAIMG B:  EGEGIWLALGTIGMLLGMLYFIADGLDVQDPRQKEFYVIT ILIPAIAAASYLSMFFGFGLTEVSLANGRVVDVYWARYAD WLFTTPLLLLDIGLLAGASQRDIGALVGIDAFMIVTGLVA TLTKVVVARYAFWTISTISMVFLLYYLVAVFGEAVSDADE DTRSTFNALRNIILVTWAIYPVAWLVGTEGLALTGLYGET LLFMVLDLVAKVGFGFILLRSRAI Description (1)  Bacteriorhodopsin Functional site 1) chain A residue 91 type sequence Y description BINDING SITE FOR RESIDUE RET A 301 source : AC1 2) chain A residue 94 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC1 3) chain A residue 98 type sequence T description BINDING SITE FOR RESIDUE RET A 301 source : AC1 4) chain A residue 126 type sequence M description BINDING SITE FOR RESIDUE RET A 301 source : AC1 5) chain A residue 130 type sequence G description BINDING SITE FOR RESIDUE RET A 301 source : AC1 6) chain A residue 146 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC1 7) chain A residue 149 type sequence S description BINDING SITE FOR RESIDUE RET A 301 source : AC1 8) chain A residue 150 type sequence T description BINDING SITE FOR RESIDUE RET A 301 source : AC1 9) chain A residue 153 type sequence M description BINDING SITE FOR RESIDUE RET A 301 source : AC1 10) chain A residue 190 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC1 11) chain A residue 193 type sequence Y description BINDING SITE FOR RESIDUE RET A 301 source : AC1 12) chain A residue 194 type sequence P description BINDING SITE FOR RESIDUE RET A 301 source : AC1 13) chain A residue 223 type sequence A description BINDING SITE FOR RESIDUE RET A 301 source : AC1 14) chain A residue 224 type sequence K description BINDING SITE FOR RESIDUE RET A 301 source : AC1 15) chain A residue 75 type sequence E description BINDING SITE FOR RESIDUE ACT A 302 source : AC2 16) chain A residue 77 type sequence S description BINDING SITE FOR RESIDUE ACT A 302 source : AC2 17) chain A residue 183 type sequence R description BINDING SITE FOR RESIDUE ACT A 303 source : AC3 18) chain B residue 79 type sequence A description BINDING SITE FOR RESIDUE ACT A 303 source : AC3 19) chain B residue 80 type sequence N description BINDING SITE FOR RESIDUE ACT A 303 source : AC3 20) chain B residue 139 type sequence V description BINDING SITE FOR RESIDUE ACT A 303 source : AC3 21) chain B residue 94 type sequence W description BINDING SITE FOR RESIDUE RET B 301 source : AC4 22) chain B residue 97 type sequence T description BINDING SITE FOR RESIDUE RET B 301 source : AC4 23) chain B residue 98 type sequence T description BINDING SITE FOR RESIDUE RET B 301 source : AC4 24) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE RET B 301 source : AC4 25) chain B residue 146 type sequence W description BINDING SITE FOR RESIDUE RET B 301 source : AC4 26) chain B residue 149 type sequence S description BINDING SITE FOR RESIDUE RET B 301 source : AC4 27) chain B residue 150 type sequence T description BINDING SITE FOR RESIDUE RET B 301 source : AC4 28) chain B residue 190 type sequence W description BINDING SITE FOR RESIDUE RET B 301 source : AC4 29) chain B residue 193 type sequence Y description BINDING SITE FOR RESIDUE RET B 301 source : AC4 30) chain B residue 194 type sequence P description BINDING SITE FOR RESIDUE RET B 301 source : AC4 31) chain B residue 197 type sequence W description BINDING SITE FOR RESIDUE RET B 301 source : AC4 32) chain B residue 224 type sequence K description BINDING SITE FOR RESIDUE RET B 301 source : AC4 33) chain B residue 114 type sequence R description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 34) chain B residue 121 type sequence G description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 35) chain B residue 173 type sequence E description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 36) chain B residue 176 type sequence R description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 37) chain B residue 177 type sequence S description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 38) chain B residue 180 type sequence N description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 39) chain B residue 181 type sequence A description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 40) chain B residue 184 type sequence N description BINDING SITE FOR RESIDUE MPG B 302 source : AC5 41) chain A residue 216-227 type prosite sequence FMVLDLVAKVGF description BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDLvAKvGF source prosite : PS00327 42) chain A residue 90-102 type prosite sequence RYADWLFTTPLLL description BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL source prosite : PS00950 43) chain A residue 16-36 type TRANSMEM sequence EGIWLALGTIGMLLGMLYFIA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 91-111 type TRANSMEM sequence YADWLFTTPLLLLDIGLLAGA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 116-136 type TRANSMEM sequence IGALVGIDAFMIVTGLVATLT description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 144-164 type TRANSMEM sequence AFWTISTISMVFLLYYLVAVF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 185-205 type TRANSMEM sequence IILVTWAIYPVAWLVGTEGLA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 212-232 type TRANSMEM sequence ETLLFMVLDLVAKVGFGFILL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 51-71 type TRANSMEM sequence VITILIPAIAAASYLSMFFGF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 91-111 type TRANSMEM sequence YADWLFTTPLLLLDIGLLAGA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 116-136 type TRANSMEM sequence IGALVGIDAFMIVTGLVATLT description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 144-164 type TRANSMEM sequence AFWTISTISMVFLLYYLVAVF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 185-205 type TRANSMEM sequence IILVTWAIYPVAWLVGTEGLA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 212-232 type TRANSMEM sequence ETLLFMVLDLVAKVGFGFILL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 16-36 type TRANSMEM sequence EGIWLALGTIGMLLGMLYFIA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 51-71 type TRANSMEM sequence VITILIPAIAAASYLSMFFGF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 93 type SITE sequence D description Primary proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 93 type SITE sequence D description Primary proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 224 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 60) chain B residue 224 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4

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