eF-site ID 5o1v-AB PDB Code 5o1v Chain A, B click to enlarge Title Crystal structure of WNK3 kinase domain in a monophosphorylated apo state (A-loop swapped) Classification STRUCTURAL GENOMICS Compound Serine/threonine-protein kinase WNK3 Source (WNK3_HUMAN) Sequence A:  EMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEV AWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSW ESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSW CRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIG DLGLATLMRTXFAKSVIGTPEFMAPEMYEEHYDESVDVYA FGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKV TDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDTGLR B:  EMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEV AWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSW ESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSW CRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIG DLGLATLMRTXGTPEFMAPEMYEEHYDESVDVYAFGMCML EMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVK EIIEGCIRQNKSERLSIRDLLNHAFFAEDTG Description (1)  FAM83B Functional site 1) chain A residue 227 type sequence T description binding site for residue EDO A 501 source : AC1 2) chain A residue 228 type sequence E description binding site for residue EDO A 501 source : AC1 3) chain A residue 230 type sequence M description binding site for residue EDO A 501 source : AC1 4) chain A residue 207 type sequence V description binding site for residue EDO A 502 source : AC2 5) chain A residue 209 type sequence F description binding site for residue EDO A 502 source : AC2 6) chain A residue 293 type sequence G description binding site for residue EDO A 502 source : AC2 7) chain A residue 294 type sequence D description binding site for residue EDO A 502 source : AC2 8) chain A residue 295 type sequence L description binding site for residue EDO A 502 source : AC2 9) chain A residue 194 type sequence E description binding site for residue EDO A 503 source : AC3 10) chain A residue 272 type sequence I description binding site for residue EDO A 503 source : AC3 11) chain A residue 273 type sequence H description binding site for residue EDO A 503 source : AC3 12) chain A residue 295 type sequence L description binding site for residue EDO A 503 source : AC3 13) chain A residue 296 type sequence G description binding site for residue EDO A 503 source : AC3 14) chain A residue 159 type sequence K description binding site for residue EDO A 504 source : AC4 15) chain A residue 161 type sequence V description binding site for residue EDO A 504 source : AC4 16) chain A residue 294 type sequence D description binding site for residue EDO A 504 source : AC4 17) chain A residue 297 type sequence L description binding site for residue EDO A 504 source : AC4 18) chain A residue 342 type sequence A description binding site for residue EDO A 505 source : AC5 19) chain A residue 364 type sequence G description binding site for residue EDO A 506 source : AC6 20) chain A residue 366 type sequence K description binding site for residue EDO A 506 source : AC6 21) chain A residue 386 type sequence I description binding site for residue EDO A 506 source : AC6 22) chain A residue 256 type sequence Q description binding site for residue EDO A 507 source : AC7 23) chain A residue 287 type sequence T description binding site for residue EDO A 507 source : AC7 24) chain A residue 289 type sequence S description binding site for residue EDO A 507 source : AC7 25) chain A residue 387 type sequence R description binding site for residue EDO A 508 source : AC8 26) chain A residue 392 type sequence E description binding site for residue EDO A 508 source : AC8 27) chain A residue 394 type sequence L description binding site for residue EDO A 508 source : AC8 28) chain A residue 342 type sequence A description binding site for residue EDO A 509 source : AC9 29) chain A residue 372 type sequence K description binding site for residue EDO A 509 source : AC9 30) chain A residue 374 type sequence T description binding site for residue EDO A 510 source : AD1 31) chain A residue 375 type sequence D description binding site for residue EDO A 510 source : AD1 32) chain B residue 137 type sequence A description binding site for residue EDO B 501 source : AD2 33) chain B residue 139 type sequence A description binding site for residue EDO B 501 source : AD2 34) chain B residue 140 type sequence T description binding site for residue EDO B 501 source : AD2 35) chain B residue 207 type sequence V description binding site for residue EDO B 502 source : AD3 36) chain B residue 227 type sequence T description binding site for residue EDO B 502 source : AD3 37) chain B residue 228 type sequence E description binding site for residue EDO B 502 source : AD3 38) chain B residue 229 type sequence L description binding site for residue EDO B 502 source : AD3 39) chain B residue 230 type sequence M description binding site for residue EDO B 502 source : AD3 40) chain B residue 251 type sequence R description binding site for residue EDO B 503 source : AD4 41) chain B residue 403 type sequence A description binding site for residue EDO B 503 source : AD4 42) chain B residue 404 type sequence F description binding site for residue EDO B 503 source : AD4 43) chain B residue 323 type sequence E description binding site for residue EDO B 504 source : AD5 44) chain B residue 324 type sequence H description binding site for residue EDO B 504 source : AD5 45) chain B residue 325 type sequence Y description binding site for residue EDO B 504 source : AD5 46) chain B residue 159 type sequence K description binding site for residue EDO B 505 source : AD6 47) chain B residue 293 type sequence G description binding site for residue EDO B 505 source : AD6 48) chain B residue 294 type sequence D description binding site for residue EDO B 505 source : AD6 49) chain A residue 286 type sequence P description binding site for residue EDO B 506 source : AD7 50) chain B residue 172 type sequence E description binding site for residue EDO B 506 source : AD7 51) chain A residue 294 type ACT_SITE sequence D description Proton acceptor => ECO:0000250|UniProtKB:Q9JIH7 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 294 type ACT_SITE sequence D description Proton acceptor => ECO:0000250|UniProtKB:Q9JIH7 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 227 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q9H4A3 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 277 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q9H4A3 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 227 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q9H4A3 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 277 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q9H4A3 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 271-283 type prosite sequence IIHRDLKCDNIFI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKcdNIFI source prosite : PS00108 58) chain A residue 308 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:33439774 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 304 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9JIH7 source Swiss-Prot : SWS_FT_FI3 60) chain B residue 304 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9JIH7 source Swiss-Prot : SWS_FT_FI3

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