eF-site ID 3b60-ABCD PDB Code 3b60 Chain A, B, C, D click to enlarge Title Crystal Structure of MsbA from Salmonella typhimurium with AMPPNP, higher resolution form Classification MEMBRANE PROTEIN Compound Lipid A export ATP-binding/permease protein msbA Source Salmonella typhimurium (MSBA_SALTY) Sequence A:  WQTFRRLWPTIAPFKAGLIVAGIALILNAASDTFMLSLLK PLLDDGFGKTDRSVLLWMPLVVIGLMILRGITSYISSYCI SWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRIT YDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSI ILVVLAPIVSIAIRVVSKRFRSISKNMQNTMGQVTTSAEQ MLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASS ISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFS SMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKD EGKRVIDRATGDLEFRNVTFTYPGREVPALRNINLKIPAG KTVALVGRSGSGKSTIASLITRFYDIDEGHILMDGHDLRE YTLASLRNQVALVSQNVHLFNDTVANNIAYARTEEYSREQ IEEAARMAYAMDFINKMDNGLDTIIGENGVLLSGGQRQRI AIARALLRDSPILILDEATSALDTESERAIQAALDELQKN RTSLVIAHRLSTIEQADEIVVVEDGIIVERGTHSELLAQH GVYAQLHKMQFG B:  WQTFRRLWPTIAPFKAGLIVAGIALILNAASDTFMLSLLK PLLDDGFGKTDRSVLLWMPLVVIGLMILRGITSYISSYCI SWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRIT YDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSI ILVVLAPIVSIAIRVVSKRFRSISKNMQNTMGQVTTSAEQ MLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASS ISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFS SMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKD EGKRVIDRATGDLEFRNVTFTYPGREVPALRNINLKIPAG KTVALVGRSGSGKSTIASLITRFYDIDEGHILMDGHDLRE YTLASLRNQVALVSQNVHLFNDTVANNIAYARTEEYSREQ IEEAARMAYAMDFINKMDNGLDTIIGENGVLLSGGQRQRI AIARALLRDSPILILDEATSALDTESERAIQAALDELQKN RTSLVIAHRLSTIEQADEIVVVEDGIIVERGTHSELLAQH GVYAQLHKMQFG C:  WQTFRRLWPTIAPFKAGLIVAGIALILNAASDTFMLSLLK PLLDDGFGKTDRSVLLWMPLVVIGLMILRGITSYISSYCI SWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRIT YDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSI ILVVLAPIVSIAIRVVSKRFRSISKNMQNTMGQVTTSAEQ MLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASS ISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFS SMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKD EGKRVIDRATGDLEFRNVTFTYPGREVPALRNINLKIPAG KTVALVGRSGSGKSTIASLITRFYDIDEGHILMDGHDLRE YTLASLRNQVALVSQNVHLFNDTVANNIAYARTEEYSREQ IEEAARMAYAMDFINKMDNGLDTIIGENGVLLSGGQRQRI AIARALLRDSPILILDEATSALDTESERAIQAALDELQKN RTSLVIAHRLSTIEQADEIVVVEDGIIVERGTHSELLAQH GVYAQLHKMQFG D:  WQTFRRLWPTIAPFKAGLIVAGIALILNAASDTFMLSLLK PLLDDGFGKTDRSVLLWMPLVVIGLMILRGITSYISSYCI SWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRIT YDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSI ILVVLAPIVSIAIRVVSKRFRSISKNMQNTMGQVTTSAEQ MLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASS ISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFS SMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKD EGKRVIDRATGDLEFRNVTFTYPGREVPALRNINLKIPAG KTVALVGRSGSGKSTIASLITRFYDIDEGHILMDGHDLRE YTLASLRNQVALVSQNVHLFNDTVANNIAYARTEEYSREQ IEEAARMAYAMDFINKMDNGLDTIIGENGVLLSGGQRQRI AIARALLRDSPILILDEATSALDTESERAIQAALDELQKN RTSLVIAHRLSTIEQADEIVVVEDGIIVERGTHSELLAQH GVYAQLHKMQFG Description Functional site 1) chain A residue 351 type sequence Y description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 2) chain A residue 378 type sequence S description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 3) chain A residue 379 type sequence G description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 4) chain A residue 380 type sequence S description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 5) chain A residue 381 type sequence G description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 6) chain A residue 382 type sequence K description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 7) chain A residue 383 type sequence S description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 8) chain A residue 384 type sequence T description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 9) chain A residue 537 type sequence H description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 10) chain B residue 480 type sequence L description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 11) chain B residue 482 type sequence S description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 12) chain B residue 484 type sequence G description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 13) chain B residue 485 type sequence Q description BINDING SITE FOR RESIDUE ANP A 5001 source : AC1 14) chain A residue 480 type sequence L description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 15) chain A residue 482 type sequence S description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 16) chain A residue 484 type sequence G description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 17) chain A residue 485 type sequence Q description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 18) chain B residue 351 type sequence Y description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 19) chain B residue 378 type sequence S description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 20) chain B residue 379 type sequence G description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 21) chain B residue 380 type sequence S description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 22) chain B residue 381 type sequence G description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 23) chain B residue 382 type sequence K description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 24) chain B residue 383 type sequence S description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 25) chain B residue 384 type sequence T description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 26) chain B residue 537 type sequence H description BINDING SITE FOR RESIDUE ANP B 5002 source : AC2 27) chain C residue 351 type sequence Y description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 28) chain C residue 378 type sequence S description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 29) chain C residue 379 type sequence G description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 30) chain C residue 380 type sequence S description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 31) chain C residue 381 type sequence G description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 32) chain C residue 382 type sequence K description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 33) chain C residue 383 type sequence S description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 34) chain C residue 384 type sequence T description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 35) chain C residue 537 type sequence H description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 36) chain D residue 480 type sequence L description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 37) chain D residue 481 type sequence L description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 38) chain D residue 482 type sequence S description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 39) chain D residue 483 type sequence G description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 40) chain D residue 484 type sequence G description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 41) chain D residue 485 type sequence Q description BINDING SITE FOR RESIDUE ANP C 5003 source : AC3 42) chain C residue 480 type sequence L description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 43) chain C residue 482 type sequence S description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 44) chain C residue 483 type sequence G description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 45) chain C residue 484 type sequence G description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 46) chain C residue 485 type sequence Q description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 47) chain D residue 351 type sequence Y description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 48) chain D residue 378 type sequence S description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 49) chain D residue 379 type sequence G description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 50) chain D residue 380 type sequence S description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 51) chain D residue 381 type sequence G description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 52) chain D residue 382 type sequence K description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 53) chain D residue 383 type sequence S description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 54) chain D residue 384 type sequence T description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 55) chain D residue 537 type sequence H description BINDING SITE FOR RESIDUE ANP D 5004 source : AC4 56) chain A residue 376 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 376 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 376 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 376 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 16-36 type TRANSMEM sequence LWPTIAPFKAGLIVAGIALIL description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 275-295 type TRANSMEM sequence VMDSLTAGTITVVFSSMIALM description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 16-36 type TRANSMEM sequence LWPTIAPFKAGLIVAGIALIL description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 64-84 type TRANSMEM sequence LLWMPLVVIGLMILRGITSYI description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 64) chain C residue 153-173 type TRANSMEM sequence IIGLFIMMFYYSWQLSIILVV description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 65) chain C residue 253-273 type TRANSMEM sequence PIIQLIASLALAFVLYAASFP description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 275-295 type TRANSMEM sequence VMDSLTAGTITVVFSSMIALM description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 67) chain D residue 16-36 type TRANSMEM sequence LWPTIAPFKAGLIVAGIALIL description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 68) chain D residue 64-84 type TRANSMEM sequence LLWMPLVVIGLMILRGITSYI description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 69) chain D residue 153-173 type TRANSMEM sequence IIGLFIMMFYYSWQLSIILVV description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 70) chain D residue 253-273 type TRANSMEM sequence PIIQLIASLALAFVLYAASFP description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 64-84 type TRANSMEM sequence LLWMPLVVIGLMILRGITSYI description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 72) chain D residue 275-295 type TRANSMEM sequence VMDSLTAGTITVVFSSMIALM description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 153-173 type TRANSMEM sequence IIGLFIMMFYYSWQLSIILVV description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 253-273 type TRANSMEM sequence PIIQLIASLALAFVLYAASFP description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 275-295 type TRANSMEM sequence VMDSLTAGTITVVFSSMIALM description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 16-36 type TRANSMEM sequence LWPTIAPFKAGLIVAGIALIL description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 77) chain B residue 64-84 type TRANSMEM sequence LLWMPLVVIGLMILRGITSYI description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 78) chain B residue 153-173 type TRANSMEM sequence IIGLFIMMFYYSWQLSIILVV description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 79) chain B residue 253-273 type TRANSMEM sequence PIIQLIASLALAFVLYAASFP description Helical => ECO:0000255|HAMAP-Rule:MF_01703 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 481-495 type prosite sequence LSGGQRQRIAIARAL description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRIAIARAL source prosite : PS00211

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