eF-site ID 5b6w-A PDB Code 5b6w Chain A click to enlarge Title A three dimensional movie of structural changes in bacteriorhodopsin: structure obtained 16 ns after photoexcitation Classification PROTON TRANSPORT Compound Bacteriorhodopsin Source ORGANISM_SCIENTIFIC: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1); Sequence A:  ITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFY AITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY ADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGL VGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESM RPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNI ETLLFMVLDVSAKVGFGLILLRSRAIFGEAE Description Functional site 1) chain A residue 86 type sequence W description binding site for residue RET A 300 source : AC1 2) chain A residue 90 type sequence T description binding site for residue RET A 300 source : AC1 3) chain A residue 118 type sequence M description binding site for residue RET A 300 source : AC1 4) chain A residue 138 type sequence W description binding site for residue RET A 300 source : AC1 5) chain A residue 141 type sequence S description binding site for residue RET A 300 source : AC1 6) chain A residue 142 type sequence T description binding site for residue RET A 300 source : AC1 7) chain A residue 182 type sequence W description binding site for residue RET A 300 source : AC1 8) chain A residue 185 type sequence Y description binding site for residue RET A 300 source : AC1 9) chain A residue 186 type sequence P description binding site for residue RET A 300 source : AC1 10) chain A residue 212 type sequence D description binding site for residue RET A 300 source : AC1 11) chain A residue 215 type sequence A description binding site for residue RET A 300 source : AC1 12) chain A residue 216 type sequence K description binding site for residue RET A 300 source : AC1 13) chain A residue 44 type sequence A description binding site for residue L2P A 600 source : AC2 14) chain A residue 48 type sequence L description binding site for residue L2P A 600 source : AC2 15) chain A residue 54 type sequence F description binding site for residue L2P A 600 source : AC2 16) chain A residue 107 type sequence T description binding site for residue L2P A 600 source : AC2 17) chain A residue 147 type sequence Y description binding site for residue L2P A 600 source : AC2 18) chain A residue 149 type sequence L description binding site for residue TRD A 601 source : AC3 19) chain A residue 22 type sequence L description binding site for residue D10 A 602 source : AC4 20) chain A residue 172 type sequence K description binding site for residue OCT A 604 source : AC6 21) chain A residue 131 type sequence Y description binding site for residue L2P A 608 source : AD1 22) chain A residue 138 type sequence W description binding site for residue L2P A 608 source : AD1 23) chain A residue 203 type sequence I description binding site for residue L2P A 608 source : AD1 24) chain A residue 52 type sequence I description binding site for residue L2P A 609 source : AD2 25) chain A residue 56 type sequence M description binding site for residue L2P A 609 source : AD2 26) chain A residue 64 type sequence Y description binding site for residue L2P A 609 source : AD2 27) chain A residue 80 type sequence W description binding site for residue L2P A 609 source : AD2 28) chain A residue 84 type sequence A description binding site for residue L2P A 609 source : AD2 29) chain A residue 116 type sequence G description binding site for residue L2P A 609 source : AD2 30) chain A residue 117 type sequence I description binding site for residue L2P A 609 source : AD2 31) chain A residue 120 type sequence G description binding site for residue L2P A 609 source : AD2 32) chain A residue 123 type sequence L description binding site for residue L2P A 609 source : AD2 33) chain A residue 123 type sequence L description binding site for residue L2P A 609 source : AD2 34) chain A residue 124 type sequence V description binding site for residue L2P A 609 source : AD2 35) chain A residue 26 type sequence Y description binding site for residue MYS A 610 source : AD3 36) chain A residue 225 type sequence R description binding site for residue DD9 A 611 source : AD4 37) chain A residue 87 type sequence L description binding site for residue C14 A 612 source : AD5 38) chain A residue 91 type sequence P description binding site for residue C14 A 612 source : AD5 39) chain A residue 95 type sequence L description binding site for residue C14 A 612 source : AD5 40) chain A residue 26 type sequence Y description binding site for residue OCT A 613 source : AD6 41) chain A residue 63-79 type TOPO_DOM sequence GYGLTMVPFGGEQNPIY description Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI1 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) chain A residue 80-96 type TRANSMEM sequence WARYADWLFTTPLLLLD description Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W source Swiss-Prot : SWS_FT_FI5 50) 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 51) 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 52) 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 53) 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 54) chain A residue 85 type SITE sequence D description Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064 source Swiss-Prot : SWS_FT_FI10 55) 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 56) chain A residue 208-219 type prosite sequence FMVLDVSAKVGF description BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVsAKvGF source prosite : PS00327 57) chain A residue 82-94 type prosite sequence RYADWLFTTPLLL description BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL source prosite : PS00950

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