eF-site ID 3lut-B PDB Code 3lut Chain 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 B:  CERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDP LRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSE EIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWL LFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDE NEDMHGGGVTFHTYSQSTIGYQQSTSFTDPFFIVETLCII WFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLG TELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHS KGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEA DERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVG SLCAIAGVLTIALPVPVIVSNFNYFYHRET Description Functional site 1) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 2) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 3) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 4) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 500 source : AC2 5) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 6) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 7) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 8) chain B residue 374 type sequence T description BINDING SITE FOR RESIDUE K B 501 source : AC3 9) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 10) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 11) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 12) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 501 source : AC3 13) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 14) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 15) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 16) chain B residue 375 type sequence V description BINDING SITE FOR RESIDUE K B 502 source : AC4 17) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 18) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 19) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 20) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 502 source : AC4 21) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 22) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 23) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 24) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE K B 503 source : AC5 25) 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 26) 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 27) 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 28) 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 29) chain B residue 244 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000255 source Swiss-Prot : SWS_FT_FI21 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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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