eF-site ID 1mgy-A PDB Code 1mgy Chain A click to enlarge Title Structure of the D85S mutant of bacteriorhodopsin with bromide bound Classification PROTON TRANSPORT Compound Bacteriorhodopsin Source Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) (BACR_HALN1) Sequence A:  ITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFY AITTLVPAIAFTMYLSMLLGYIYWARYASWLFTTPLLLLD LALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFV WWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRN VTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAK VGFGLILLRSRAIFGE Description Functional site 1) chain A residue 85 type sequence S description BINDING SITE FOR RESIDUE BR A 901 source : AC1 2) chain A residue 212 type sequence D description BINDING SITE FOR RESIDUE BR A 901 source : AC1 3) chain A residue 216 type sequence K description BINDING SITE FOR RESIDUE BR A 901 source : AC1 4) chain A residue 104 type sequence D description BINDING SITE FOR RESIDUE BR A 902 source : AC2 5) chain A residue 107 type sequence T description BINDING SITE FOR RESIDUE BR A 902 source : AC2 6) chain A residue 159 type sequence K description BINDING SITE FOR RESIDUE BR A 902 source : AC2 7) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE K A 802 source : AC3 8) chain A residue 230 type sequence F description BINDING SITE FOR RESIDUE K A 802 source : AC3 9) chain A residue 86 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC4 10) chain A residue 89 type sequence T description BINDING SITE FOR RESIDUE RET A 301 source : AC4 11) chain A residue 90 type sequence T description BINDING SITE FOR RESIDUE RET A 301 source : AC4 12) chain A residue 118 type sequence M description BINDING SITE FOR RESIDUE RET A 301 source : AC4 13) chain A residue 138 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC4 14) chain A residue 141 type sequence S description BINDING SITE FOR RESIDUE RET A 301 source : AC4 15) chain A residue 182 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC4 16) chain A residue 185 type sequence Y description BINDING SITE FOR RESIDUE RET A 301 source : AC4 17) chain A residue 189 type sequence W description BINDING SITE FOR RESIDUE RET A 301 source : AC4 18) chain A residue 212 type sequence D description BINDING SITE FOR RESIDUE RET A 301 source : AC4 19) chain A residue 216 type sequence K description BINDING SITE FOR RESIDUE RET A 301 source : AC4 20) chain A residue 105 type sequence Q description BINDING SITE FOR RESIDUE LI1 A 601 source : AC5 21) chain A residue 108 type sequence I description BINDING SITE FOR RESIDUE LI1 A 601 source : AC5 22) chain A residue 199 type sequence V description BINDING SITE FOR RESIDUE LI1 A 601 source : AC5 23) chain A residue 56 type sequence M description BINDING SITE FOR RESIDUE LI1 A 602 source : AC6 24) chain A residue 132 type sequence S description BINDING SITE FOR RESIDUE LI1 A 603 source : AC7 25) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE LI1 A 603 source : AC7 26) chain A residue 40 type sequence K description BINDING SITE FOR RESIDUE LI1 A 605 source : AC8 27) chain A residue 5 type sequence T description BINDING SITE FOR RESIDUE LI1 A 608 source : AC9 28) chain A residue 10 type sequence W description BINDING SITE FOR RESIDUE LI1 A 608 source : AC9 29) chain A residue 18 type sequence A description BINDING SITE FOR RESIDUE LI1 A 608 source : AC9 30) chain A residue 109 type sequence L description BINDING SITE FOR RESIDUE LI1 A 608 source : AC9 31) chain A residue 202 type sequence N description BINDING SITE FOR RESIDUE LI1 A 608 source : AC9 32) chain A residue 203 type sequence I description BINDING SITE FOR RESIDUE LI1 A 608 source : AC9 33) chain A residue 173-191 type TRANSMEM sequence VLRNVTVVLWSAYPVVWLI description Helical; Name=Helix F => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI8 34) chain A residue 63-79 type TOPO_DOM sequence GYIY description Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI1 35) chain A residue 128-134 type TOPO_DOM sequence TKVYSYR description Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI1 36) chain A residue 192-203 type TOPO_DOM sequence GSEGAGIVPLNI description Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI1 37) chain A residue 10-29 type TRANSMEM sequence WIWLALGTALMGLGTLYFLV description Helical; Name=Helix A => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI2 38) chain A residue 30-43 type TOPO_DOM sequence KGMGVSDPDAKKFY description Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI3 39) chain A residue 97-107 type TOPO_DOM sequence LALLVDADQGT description Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI3 40) chain A residue 155-172 type TOPO_DOM sequence GFTSKAESMRPEVASTFK description Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI3 41) chain A residue 44-62 type TRANSMEM sequence AITTLVPAIAFTMYLSMLL description Helical; Name=Helix B => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI4 42) chain A residue 80-96 type TRANSMEM sequence WARYASWLFTTPLLLLD description Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI5 43) chain A residue 108-127 type TRANSMEM sequence ILALVGADGIMIGTGLVGAL description Helical; Name=Helix D => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI6 44) chain A residue 135-154 type TRANSMEM sequence FVWWAISTAAMLYILYVLFF description Helical; Name=Helix E => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI7 45) chain A residue 216 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112, ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949307, ECO:0000269|PubMed:10949309, ECO:0000269|PubMed:11829498, ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6794028, ECO:0000269|PubMed:9287223, ECO:0000269|PubMed:9632391, ECO:0000269|PubMed:9751724, ECO:0007744|PDB:1C3W, ECO:0007744|PDB:1F50, ECO:0007744|PDB:1IW9, ECO:0007744|PDB:1KG8, ECO:0007744|PDB:1KG9, ECO:0007744|PDB:1M0L, ECO:0007744|PDB:1M0M, ECO:0007744|PDB:1O0A, ECO:0007744|PDB:1P8H, ECO:0007744|PDB:1P8U, ECO:0007744|PDB:1Q5J, ECO:0007744|PDB:1QHJ, ECO:0007744|PDB:1QKP, ECO:0007744|PDB:1QM8, ECO:0007744|PDB:1R2N, ECO:0007744|PDB:1R84, ECO:0007744|PDB:1S8J, ECO:0007744|PDB:1TN0, ECO:0007744|PDB:1TN5, ECO:0007744|PDB:1UCQ, ECO:0007744|PDB:1X0I, ECO:0007744|PDB:1X0K, ECO:0007744|PDB:1X0S, ECO:0007744|PDB:1XJI, ECO:0007744|PDB:2AT9, ECO:0007744|PDB:2BRD, ECO:0007744|PDB:2I1X, ECO:0007744|PDB:2I20, ECO:0007744|PDB:2I21, ECO:0007744|PDB:2NTU, ECO:0007744|PDB:2NTW, ECO:0007744|PDB:2WJK, ECO:0007744|PDB:2WJL, ECO:0007744|PDB:2ZFE, ECO:0007744|PDB:2ZZL, ECO:0007744|PDB:3COD, ECO:0007744|PDB:3HAN, ECO:0007744|PDB:3HAO, ECO:0007744|PDB:3HAP, ECO:0007744|PDB:3HAQ, ECO:0007744|PDB:3HAR, ECO:0007744|PDB:3HAS, ECO:0007744|PDB:3NS0, ECO:0007744|PDB:3NSB, ECO:0007744|PDB:3T45, ECO:0007744|PDB:3UTV, ECO:0007744|PDB:3UTW, ECO:0007744|PDB:3UTX, ECO:0007744|PDB:3VHZ, ECO:0007744|PDB:3VI0, ECO:0007744|PDB:4FPD, ECO:0007744|PDB:4HWL, ECO:0007744|PDB:4MD1, ECO:0007744|PDB:4MD2, ECO:0007744|PDB:4X31, ECO:0007744|PDB:4X32, ECO:0007744|PDB:5A44, ECO:0007744|PDB:5A45, ECO:0007744|PDB:5B34, ECO:0007744|PDB:5B6V, ECO:0007744|PDB:5B6W, ECO:0007744|PDB:5B6X, ECO:0007744|PDB:5B6Y, ECO:0007744|PDB:5B6Z, ECO:0007744|PDB:5BR2, ECO:0007744|PDB:5BR5, ECO:0007744|PDB:5H2H, ECO:0007744|PDB:5H2I, ECO:0007744|PDB:5H2J, ECO:0007744|PDB:5H2K, ECO:0007744|PDB:5H2L, ECO:0007744|PDB:5H2M, ECO:0007744|PDB:5H2N, ECO:0007744|PDB:5H2O, ECO:0007744|PDB:5H2P, ECO:0007744|PDB:5J7A source Swiss-Prot : SWS_FT_FI12 46) chain A residue 204-223 type TRANSMEM sequence ETLLFMVLDVSAKVGFGLIL description Helical; Name=Helix G => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI9 47) chain A residue 208-219 type prosite sequence FMVLDVSAKVGF description BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVsAKvGF source prosite : PS00327 48) chain A residue 85 type SITE sequence S description Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064 source Swiss-Prot : SWS_FT_FI10

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