eF-site ID 6jxj-AB PDB Code 6jxj Chain A, B click to enlarge Title Rb+-bound E2-AlF state of the gastric proton pump (Tyr799Trp) Classification MEMBRANE PROTEIN Compound Potassium-transporting ATPase alpha chain 1 Source (ATP4B_PIG) Sequence A:  GMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGP NALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAI QASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNI IASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGD RVPADIRILQAQGCKVDNSSLTGESEPQTRSPECTHESPL ETRNIAFFSTMCLEGTAQGLVVNTGDRTIIGRIASLASGV ENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTF LRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCV VKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHI HSADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQ DAVPVPKRIVIGDASETALLKFSELTLGNAMGYRERFPKV CEIPFNSTNKFQLSIHTLEDPRDPRHVLVMKGAPERVLER CSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQ LYLSEKDYPPGYAFDVEAMNFPTSGLCFAGLVSMIDPPRA TVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEG SETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSE LVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGD GVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFAS IVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPWLIYITVS VPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPR NPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEG WFPLLCVGLRPQWENHHLQDLQDSYGQEWTFGQRLYQQYT CYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVI AIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFSL LIFVYDEIRKLGVRCCPGSWWDQELYY B:  MLGRTLSRWVWISLYYVAFYVVMSGIFALCIYVLMRTIDP YTPDYQDQLKSPGVTLRPDVYGEKGLDISYNVSDSTTWAG LAHTLHRFLAGYSPAAQEGSINCTSEKYFFQESFLAPNHT KFSCKFTADMLQNCSGRPDPTFGFAEGKPCFIIKMNRIVK FLPGNSTAPRVDCAFLDQPRDGPPLQVEYFPANGTYSLHY FPYYGKKAQPHYSNPLVAAKLLNVPRNRDVVIVCKILAEH VSFDNPHDPYEGKVEFKLKIQK Description Functional site 1) chain A residue 838 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09626 source Swiss-Prot : SWS_FT_FI10 2) chain A residue 952 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250 source Swiss-Prot : SWS_FT_FI11 3) chain B residue 149-164 type prosite sequence KFSCKFTADMLQNCSG description ATPASE_NA_K_BETA_2 Sodium and potassium ATPases beta subunits signature 2. KfsCKftadmLqnCSG source prosite : PS00391 4) chain A residue 385-391 type prosite sequence DKTGTLT description ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT source prosite : PS00154 5) chain B residue 37-57 type TRANSMEM sequence WVWISLYYVAFYVVMSGIFAL description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 141-161 type TRANSMEM sequence LALALIAVVVVTGCFGYYQEF description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 298-317 type TRANSMEM sequence EHFVDIIAGLAILFGATFFI description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 330-347 type TRANSMEM sequence MVFFMAIVVAYVPEGLLA description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 782-801 type TRANSMEM sequence KKSIAYTLTKNIPELTPWLI description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 812-832 type TRANSMEM sequence GCITILFIELCTDIFPSVSLA description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 853-875 type TRANSMEM sequence LVNEPLAAYSYFQIGAIQSFAGF description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 928-947 type TRANSMEM sequence YTVFFISIEMCQIADVLIRK description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 962-980 type TRANSMEM sequence RILVIAIVFQVCIGCFLCY description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 996-1016 type TRANSMEM sequence QWWLVPMPFSLLIFVYDEIRK description Helical; Signal-anchor for type II membrane protein => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 58-290 type TOPO_DOM sequence CIYVLMRTIDPYTPDYQDQLKSPGVTLRPDVYGEKGLDIS YNVSDSTTWAGLAHTLHRFLAGYSPAAQEGSINCTSEKYF FQESFLAPNHTKFSCKFTADMLQNCSGRPDPTFGFAEGKP CFIIKMNRIVKFLPGNSTAPRVDCAFLDQPRDGPPLQVEY FPANGTYSLHYFPYYGKKAQPHYSNPLVAAKLLNVPRNRD VVIVCKILAEHVSFDNPHDPYEGKVEFKLKIQK description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 318-329 type TOPO_DOM sequence VAMCIGYTFLRA description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 802-811 type TOPO_DOM sequence YITVSVPLPL description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 876-927 type TOPO_DOM sequence TDYFTAMAQEGWFPLLCVGLRPQWENHHLQDLQDSYGQEW TFGQRLYQQYTC description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 981-995 type TOPO_DOM sequence CPGMPNIFNFMPIRF description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 99 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P18597 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 130 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P18597 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P18597 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 161 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P18597 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 193 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P18597 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 221 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P18597 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 385 type ACT_SITE sequence D description 4-aspartylphosphate intermediate => ECO:0000269|PubMed:1720615 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 343 type BINDING sequence E description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI5 28) chain A residue 795 type BINDING sequence E description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI5 29) chain A residue 820 type BINDING sequence E description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI5 30) chain A residue 338 type BINDING sequence V description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI5 31) chain A residue 339 type BINDING sequence A description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI5 32) chain A residue 341 type BINDING sequence V description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI5 33) chain A residue 385 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI6 34) chain A residue 387 type BINDING sequence T description BINDING => ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI6 35) chain A residue 726 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH source Swiss-Prot : SWS_FT_FI6 36) chain A residue 730 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 37) chain A residue 461 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PIE5 source Swiss-Prot : SWS_FT_FI8 38) chain A residue 599 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P50993 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links