eF-site ID 3c1h-A PDB Code 3c1h Chain A click to enlarge Title Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB Classification TRANSPORT PROTEIN Compound Ammonia channel Source Escherichia coli (strain K12) (AMTB_ECOLI) Sequence A:  AVADKADNAFMMICTALVLFMTIPGIALFYGGLIRGKNVL SMLTQVTVTFALVCILWVVYGYSLAFGEGNNFFGNINWLM LKNIELTAVMGSIYQYIHVAFQGSAACITVGLIVGALAER IRFSAVLIFVVVWLTLSYIPIAHMVWGGGLLASHGALDFA GGTVVHINAAIAGLVGAYLPHNLPMVFTGTAILYIGWFGF NAGSAGTANEIAALAFVNTVVATAAAILGWIFGEWALRGK PSLLGACSGAIAGLVGVTPACGYIGVGGALIIGVVAGLAG LWGVTMDPCDVFGVHGVCGIVGCIMTGIFAASSLGGVGFA EGVTMGHQLLVQLESIAITIVWSGVVAFIGYKLADLTVGL RVP Description Functional site 1) chain A residue 158 type sequence A description BINDING SITE FOR RESIDUE ACT A 425 source : AC1 2) chain A residue 159 type sequence L description BINDING SITE FOR RESIDUE ACT A 425 source : AC1 3) chain A residue 160 type sequence D description BINDING SITE FOR RESIDUE ACT A 425 source : AC1 4) chain A residue 278 type sequence Y description BINDING SITE FOR RESIDUE ACT A 425 source : AC1 5) chain A residue 28 type sequence I description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 6) chain A residue 31 type sequence F description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 7) chain A residue 110 type sequence I description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 8) chain A residue 162 type sequence A description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 9) chain A residue 168 type sequence H description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 10) chain A residue 212 type sequence W description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 11) chain A residue 215 type sequence F description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 12) chain A residue 312 type sequence C description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 13) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 14) chain A residue 318 type sequence H description BINDING SITE FOR RESIDUE LDA A 426 source : AC2 15) chain A residue 100 type sequence H description BINDING SITE FOR RESIDUE IMD A 427 source : AC3 16) chain A residue 103 type sequence F description BINDING SITE FOR RESIDUE IMD A 427 source : AC3 17) chain A residue 218 type sequence G description BINDING SITE FOR RESIDUE IMD A 427 source : AC3 18) chain A residue 219 type sequence S description BINDING SITE FOR RESIDUE IMD A 427 source : AC3 19) chain A residue 221 type sequence G description BINDING SITE FOR RESIDUE IMD A 427 source : AC3 20) chain A residue 69-97 type TOPO_DOM sequence GEGNNFFGNINWLMLKNIELTAVMGSIYQ description Periplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 150-163 type TOPO_DOM sequence GGLLASHGALDFAG description Periplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 220-226 type TOPO_DOM sequence AGTANEI description Periplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 279-280 type TOPO_DOM sequence IG description Periplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 334-348 type TOPO_DOM sequence ASSLGGVGFAEGVTM description Periplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 215 type SITE sequence F description Important for optimum substrate conductance => ECO:0000305|PubMed:18362341 source Swiss-Prot : SWS_FT_FI8 26) chain A residue 11-32 type TRANSMEM sequence AFMMICTALVLFMTIPGIALFY description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 312-333 type TRANSMEM sequence CDVFGVHGVCGIVGCIMTGIFA description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 349-377 type TRANSMEM sequence GHQLLVQLESIAITIVWSGVVAFIGYKLA description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 44-68 type TRANSMEM sequence MLTQVTVTFALVCILWVVYGYSLAF description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 98-120 type TRANSMEM sequence YIHVAFQGSAACITVGLIVGALA description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 125-149 type TRANSMEM sequence FSAVLIFVVVWLTLSYIPIAHMVWG description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 164-179 type TRANSMEM sequence GTVVHINAAIAGLVGA description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 200-219 type TRANSMEM sequence MVFTGTAILYIGWFGFNAGS description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 227-251 type TRANSMEM sequence AALAFVNTVVATAAAILGWIFGEWA description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 258-278 type TRANSMEM sequence LLGACSGAIAGLVGVTPACGY description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 281-299 type TRANSMEM sequence VGGALIIGVVAGLAGLWGV description Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 33-43 type TOPO_DOM sequence GGLIRGKNVLS description Cytoplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 121-124 type TOPO_DOM sequence ERIR description Cytoplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 180-199 type TOPO_DOM sequence YLPHNLP description Cytoplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 252-257 type TOPO_DOM sequence LRGKPS description Cytoplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 300-311 type TOPO_DOM sequence TMDP description Cytoplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 160 type SITE sequence D description Important for the deprotonation of the ammonium cation => ECO:0000269|PubMed:19278252 source Swiss-Prot : SWS_FT_FI6 43) chain A residue 168 type SITE sequence H description Twin-His motif. Important for optimum substrate conductance => ECO:0000305|PubMed:17040913, ECO:0000305|PubMed:23667517, ECO:0000305|PubMed:32662768 source Swiss-Prot : SWS_FT_FI7 44) chain A residue 318 type SITE sequence H description Twin-His motif. Important for optimum substrate conductance => ECO:0000305|PubMed:17040913, ECO:0000305|PubMed:23667517, ECO:0000305|PubMed:32662768 source Swiss-Prot : SWS_FT_FI7 45) chain A residue 219 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15361618 source Swiss-Prot : SWS_FT_FI5

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