eF-site ID 4umw-A PDB Code 4umw Chain A click to enlarge Title CRYSTAL STRUCTURE OF A ZINC-TRANSPORTING PIB-TYPE ATPASE IN E2.PI STATE Classification HYDROLASE Compound ZINC-TRANSPORTING ATPASE Source null (Q3YW59_SHISS) Sequence A:  RLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVG LYPIARQALRLIKSGSYFAIETLMSVAAIGALFIGATAEA AMVLLLFLIGERLEGWAASRVSALMALKPETATRLRNGER EEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESAL TGESIPVERATGDKVPAGATSVDRLVTLEVLSEPGASAID RILKLIEEAEERRAPIERFIDRFSRIYTPAIMAVALLVTL VPPLLFAASWQEWIYKGLTLLLIGCPCALVISTPAAITSG LAAAARRGALIKGGAALEQLGRVTQVAFDKTGTLTVGKPR VTAIHPATGISESELLTLAAAVEQGATHPLAQAIVREAQV AELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHPADA FAGLINELESAGQTVVLVVRNDDVLGIIALQDTLRADAAT AISELNALGVKGVILTGDNPRAAAAIAGELGLEFKAGLLP EDKVKAVTKLNQHAPLAMVGDGINDAPAMKAAAIGIAMGS GTDVALETADAALTHNHLRGLVQMIELARATHANIRQNIT IALGLKGIFLVTTLLGMTGLWLAVLADTGATVLVTANALR LLR Description Functional site 1) chain A residue 288 type sequence T description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 2) chain A residue 289 type sequence G description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 3) chain A residue 436 type sequence D description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 4) chain A residue 437 type sequence K description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 5) chain A residue 438 type sequence T description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 6) chain A residue 583 type sequence T description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 7) chain A residue 584 type sequence G description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 8) chain A residue 610 type sequence K description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 9) chain A residue 628 type sequence D description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 10) chain A residue 631 type sequence N description BINDING SITE FOR RESIDUE ALF A 1731 source : AC1 11) chain A residue 436 type sequence D description BINDING SITE FOR RESIDUE MG A 1732 source : AC2 12) chain A residue 438 type sequence T description BINDING SITE FOR RESIDUE MG A 1732 source : AC2 13) chain A residue 628 type sequence D description BINDING SITE FOR RESIDUE MG A 1732 source : AC2 14) chain A residue 632 type sequence D description BINDING SITE FOR RESIDUE MG A 1732 source : AC2 15) chain A residue 168-179 type TOPO_DOM sequence ARQALRLIKSGS description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 223-356 type TOPO_DOM sequence RVSALMALKPETATRLRNGEREEVAINSLRPGDVIEVAAG GRLPADGKLLSPFASFDESALTGESIPVERATGDKVPAGA TSVDRLVTLEVLSEPGASAIDRILKLIEEAEERRAPIERF IDRFSRIYTP description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 405-685 type TOPO_DOM sequence TSGLAAAARRGALIKGGAALEQLGRVTQVAFDKTGTLTVG KPRVTAIHPATGISESELLTLAAAVEQGATHPLAQAIVRE AQVAELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHP ADAFAGLINELESAGQTVVLVVRNDDVLGIIALQDTLRAD AATAISELNALGVKGVILTGDNPRAAAAIAGELGLEFKAG LLPEDKVKAVTKLNQHAPLAMVGDGINDAPAMKAAAIGIA MGSGTDVALETADAALTHNHLRGLVQMIELARATHANIRQ N description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 125-145 type TRANSMEM sequence LKENLPLITLIVMMAISWGLE description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 147-167 type TRANSMEM sequence FNHPFGQLAFIATTLVGLYPI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 180-197 type TRANSMEM sequence YFAIETLMSVAAIGALFI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 203-222 type TRANSMEM sequence AAMVLLLFLIGERLEGWAAS description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 357-377 type TRANSMEM sequence AIMAVALLVTLVPPLLFAASW description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 384-404 type TRANSMEM sequence GLTLLLIGCPCALVISTPAAI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 686-702 type TRANSMEM sequence ITIALGLKGIFLVTTLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 708-729 type TRANSMEM sequence WLAVLADTGATVLVTANALRLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 198-202 type TOPO_DOM sequence GATAE description Periplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 378-383 type TOPO_DOM sequence QEWIYK description Periplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 703-707 type TOPO_DOM sequence GMTGL description Periplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 146 type TOPO_DOM sequence Q description Periplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 436 type ACT_SITE sequence D description 4-aspartylphosphate intermediate => ECO:0000305|PubMed:25132545 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 392 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P37617 source Swiss-Prot : SWS_FT_FI6 32) chain A residue 394 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P37617 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 628 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25132545 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 436 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25132545 source Swiss-Prot : SWS_FT_FI8 35) chain A residue 438 type BINDING sequence T description BINDING => ECO:0000269|PubMed:25132545 source Swiss-Prot : SWS_FT_FI8 36) chain A residue 714 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P37617, ECO:0000305|PubMed:25132545 source Swiss-Prot : SWS_FT_FI9 37) chain A residue 711-722 type prosite sequence VLADTGATVLVT description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLADTGATVLVT source prosite : PS00141 38) chain A residue 436-442 type prosite sequence DKTGTLT description ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT source prosite : PS00154 39) chain A residue 626-648 type prosite sequence VGDGINDAPAMKAAAIGIAMGSG description COF_2 Hypothetical cof family signature 2. VGDGiNDapaMkaAaiGiaMgsG source prosite : PS01229 40) chain A residue 693 type SITE sequence K description Important for metal transport => ECO:0000305|PubMed:25132545 source Swiss-Prot : SWS_FT_FI10

Display surface Download Links