eF-site ID 3lut-A PDB Code 3lut Chain A click to enlarge 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 null (KCNA2_RAT) Sequence A:  LQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTL AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI TTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVV FANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI MEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHK IGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKD KILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNE GVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSIL GNKPYS 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 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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

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