eF-site ID 5x9h-A PDB Code 5x9h Chain A click to enlarge Title Crystal structure of the Mg2+ channel MgtE in complex with ATP Classification METAL TRANSPORT Compound Magnesium transporter MgtE Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (MGTE_THET8) Sequence A:  EVLEEIHPQDLLALWDELKGEHRYVVLTLLPKAKAAEVLS HLSPEEQAEYLKTLPPWRLREILEELSLDDLADALQAVRK EDPAYFQRLKDLLDPRTRAEVEALARYEEDEAGGLMTPEY VAVREGMTVEEVLRFLRRAAPDAETIYYIYVVDEKGRLKG VLSLRDLIVADPRTRVAEIMNPKVVYVRTDTDQEEVARLM ADYDFTVLPVVDEEGRLVGIVTVDDVLDVLEAEATEDIHK LGAVDVPDLVYSEAGPVALWLARVRWLVILILTGMVTSSI LQGFESVLEAVTALAFYVPVLLGTGGNTGNQSATLIIRAL ATRDLDLRDWRRVFLKEMGVGLLLGLTLSFLLVGKVYWDG HPLLLPVVGVSLVLIVFFANLVGAMLPFLLRRLGVDPALV SNPLVATLSDVTGLLIYLSVARLLLEA Description Functional site 1) chain A residue 170 type sequence Y description binding site for residue ATP A 501 source : AC1 2) chain A residue 183 type sequence V description binding site for residue ATP A 501 source : AC1 3) chain A residue 185 type sequence S description binding site for residue ATP A 501 source : AC1 4) chain A residue 187 type sequence R description binding site for residue ATP A 501 source : AC1 5) chain A residue 203 type sequence N description binding site for residue ATP A 501 source : AC1 6) chain A residue 205 type sequence K description binding site for residue ATP A 501 source : AC1 7) chain A residue 206 type sequence V description binding site for residue ATP A 501 source : AC1 8) chain A residue 207 type sequence V description binding site for residue ATP A 501 source : AC1 9) chain A residue 227 type sequence F description binding site for residue ATP A 501 source : AC1 10) chain A residue 231 type sequence P description binding site for residue ATP A 501 source : AC1 11) chain A residue 432 type sequence D description binding site for residue MG A 502 source : AC2 12) chain A residue 259 type sequence D description binding site for residue MG A 504 source : AC3 13) chain A residue 91 type sequence D description binding site for residue MG A 505 source : AC4 14) chain A residue 247 type sequence D description binding site for residue MG A 505 source : AC4 15) chain A residue 223 type sequence A description binding site for residue MG A 506 source : AC5 16) chain A residue 226 type sequence D description binding site for residue MG A 506 source : AC5 17) chain A residue 95 type sequence D description binding site for residue MG A 507 source : AC6 18) chain A residue 136 type sequence G description binding site for residue MG A 507 source : AC6 19) chain A residue 59 type sequence E description binding site for residue MG A 508 source : AC7 20) chain A residue 226 type sequence D description binding site for residue MG A 509 source : AC8 21) chain A residue 166 type sequence E description binding site for residue ATP B 501 source : AC9 22) chain A residue 169 type sequence Y description binding site for residue ATP B 501 source : AC9 23) chain A residue 428 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19798051 source Swiss-Prot : SWS_FT_FI10 24) chain A residue 338-351 type TOPO_DOM sequence IIRALATRDLDLRD description Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 410-420 type TOPO_DOM sequence FLLRRLGVDPA description Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 352-381 type TRANSMEM sequence WRRVFLKEMGVGLLLGLTLSFLLVGKVYWD description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB source Swiss-Prot : SWS_FT_FI2 27) chain A residue 386-409 type TRANSMEM sequence LLPVVGVSLVLIVFFANLVGAMLP description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB source Swiss-Prot : SWS_FT_FI2 28) chain A residue 421-443 type TRANSMEM sequence LVSNPLVATLSDVTGLLIYLSVA description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB source Swiss-Prot : SWS_FT_FI2 29) chain A residue 284-306 type TRANSMEM sequence ARVRWLVILILTGMVTSSILQGF description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB source Swiss-Prot : SWS_FT_FI2 30) chain A residue 316-337 type TRANSMEM sequence LAFYVPVLLGTGGNTGNQSATL description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB source Swiss-Prot : SWS_FT_FI2 31) chain A residue 307-315 type TOPO_DOM sequence ESVLEAVTA description Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 382-385 type TOPO_DOM sequence GHPL description Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 255 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 258 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 432 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 59 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 216 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 136 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI5 39) chain A residue 247 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI5 40) chain A residue 91 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI5 41) chain A residue 95 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI5 42) chain A residue 187 type BINDING sequence R description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI6 43) chain A residue 188 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI6 44) chain A residue 207 type BINDING sequence V description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI6 45) chain A residue 170 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI6 46) chain A residue 185 type BINDING sequence S description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI6 47) chain A residue 250 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI7 48) chain A residue 223 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI7 49) chain A residue 226 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H source Swiss-Prot : SWS_FT_FI7 50) chain A residue 259 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9 source Swiss-Prot : SWS_FT_FI8 51) chain A residue 418 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 383 type BINDING sequence H description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N source Swiss-Prot : SWS_FT_FI9 53) chain A residue 304 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N source Swiss-Prot : SWS_FT_FI9 54) chain A residue 307 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N source Swiss-Prot : SWS_FT_FI9 55) chain A residue 311 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N source Swiss-Prot : SWS_FT_FI9 56) chain A residue 275 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N source Swiss-Prot : SWS_FT_FI9

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