eF-site ID 3lut-AB PDB Code 3lut Chain A, B Title A Structural Model for the Full-length Shaker Potassium Channel Kv1.2 Classification MEMBRANE PROTEIN Compound Voltage-gated potassium channel subunit beta-2 Source Rattus norvegicus (Rat) (KCNA2_RAT) Sequence A:  LQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTL AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI TTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVV FANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI MEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHK IGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKD KILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNE GVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSIL GNKPYS B:  CERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDP LRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSE EIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWL LFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDE NEDMHGGGVTFHTYSQSTIGYQQSTSFTDPFFIVETLCII WFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLG TELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHS KGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEA DERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVG SLCAIAGVLTIALPVPVIVSNFNYFYHRET Description Functional site 1) chain A residue 55 type sequence G description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 2) chain A residue 56 type sequence T description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 3) chain A residue 57 type sequence W description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 4) chain A residue 63 type sequence Q description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 5) chain A residue 85 type sequence D description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 6) chain A residue 90 type sequence Y description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 7) chain A residue 158 type sequence N description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 8) chain A residue 188 type sequence S description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 9) chain A residue 189 type sequence R description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 10) chain A residue 214 type sequence Q description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 11) chain A residue 243 type sequence W description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 12) chain A residue 244 type sequence S description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 13) chain A residue 245 type sequence P description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 14) chain A residue 246 type sequence L description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 15) chain A residue 247 type sequence A description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 16) chain A residue 248 type sequence C description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 17) chain A residue 249 type sequence G description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 18) chain A residue 252 type sequence S description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 19) chain A residue 254 type sequence K description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 20) chain A residue 264 type sequence R description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 21) chain A residue 321 type sequence L description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 22) chain A residue 323 type sequence G description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 23) chain A residue 325 type sequence S description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 24) chain A residue 329 type sequence Q description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 25) chain A residue 332 type sequence E description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 26) chain A residue 333 type sequence N description BINDING SITE FOR RESIDUE NAP A 368 source : AC1 27) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 28) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 29) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 30) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 31) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 32) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 33) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 34) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 35) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 36) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 37) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 38) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 39) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 40) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 41) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 42) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 43) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 44) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 45) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 46) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 47) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 48) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 49) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 50) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 51) chain B residue 244-254 type TOPO_DOM sequence CPSKAGFFTNI description Cytoplasmic => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 311-325 type TOPO_DOM sequence SKGLQILGQTLKASM description Cytoplasmic => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI1 53) chain B residue 374-381 type INTRAMEM sequence TVGYGDMV description INTRAMEM => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI10 54) chain B residue 326-347 type TRANSMEM sequence RELGLLIFFLFIGVILFSSAVY description Helical; Name=Segment S5 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI8 55) chain B residue 244 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000255 source Swiss-Prot : SWS_FT_FI21 56) chain B residue 207 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:16770729 source Swiss-Prot : SWS_FT_FI22 57) chain B residue 389-417 type TRANSMEM sequence IVGSLCAIAGVLTIALPVPVIVSNFNYFY description Helical; Name=Segment S6 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI11 58) chain B residue 252 type SITE sequence T description Important for normal, slow channel gating => ECO:0000269|PubMed:17766348 source Swiss-Prot : SWS_FT_FI13 59) chain B residue 381 type SITE sequence V description Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxin => ECO:0000305|PubMed:25514171 source Swiss-Prot : SWS_FT_FI14 60) chain B residue 161-182 type TRANSMEM sequence PARIIAIVSVMVILISIVSFCL description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 254 type TRANSMEM sequence K description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 62) chain A residue 264 type TRANSMEM sequence R description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 325 type TRANSMEM sequence S description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 64) chain A residue 329 type TRANSMEM sequence Q description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 65) chain A residue 333 type TRANSMEM sequence N description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 66) chain A residue 57 type TRANSMEM sequence W description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 63 type TRANSMEM sequence Q description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 68) chain A residue 85 type TRANSMEM sequence D description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 188 type TRANSMEM sequence S description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 70) chain A residue 214 type TRANSMEM sequence Q description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 71) chain A residue 243 type TRANSMEM sequence W description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 72) chain A residue 244 type TRANSMEM sequence S description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 73) chain A residue 246 type TRANSMEM sequence L description Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI2 74) chain B residue 183-221 type TOPO_DOM sequence ETLPIFRDENEDMHGGGVTFHTYSQSTIGYQQSTSFTDP description Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430, ECO:0000305|PubMed:12151401 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 222-243 type TRANSMEM sequence FFIVETLCIIWFSFEFLVRFFA description Helical; Name=Segment S2 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI4 76) chain B residue 255-275 type TRANSMEM sequence MNIIDIVAIIPYFITLGTELA description Helical; Name=Segment S3 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI5 77) chain B residue 276-289 type TOPO_DOM sequence EKPEDAQQGQQAMS description Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI6 78) chain B residue 348-361 type TOPO_DOM sequence FAEADERDSQFPSI description Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI6 79) chain B residue 382-388 type TOPO_DOM sequence PTTIGGK description Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI6 80) chain B residue 290-310 type TRANSMEM sequence LAILRVIRLVRVFRIFKLSRH description Helical; Voltage-sensor; Name=Segment S4 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI7 81) chain B residue 362-373 type INTRAMEM sequence PDAFWWAVVSMT description Helical; Name=Pore helix => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 source Swiss-Prot : SWS_FT_FI9

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