eF-site ID 2wtv-B PDB Code 2wtv Chain B click to enlarge Title Aurora-A Inhibitor Structure Classification TRANSFERASE Compound SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1 Source Homo sapiens (Human) (STK6_HUMAN) Sequence B:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPRGEVYKELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR RXXLXGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK HNPSQRPMLREVLEHPWITANSSK Description Functional site 1) chain B residue 139 type sequence L description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 2) chain B residue 141 type sequence K description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 3) chain B residue 147 type sequence V description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 4) chain B residue 162 type sequence K description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 5) chain B residue 194 type sequence L description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 6) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 7) chain B residue 212 type sequence Y description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 8) chain B residue 213 type sequence A description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 9) chain B residue 261 type sequence N description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 10) chain B residue 263 type sequence L description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 11) chain B residue 273 type sequence A description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 12) chain B residue 274 type sequence D description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 13) chain B residue 275 type sequence F description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 14) chain B residue 138 type sequence P description BINDING SITE FOR RESIDUE DMS B 1391 source : AC8 15) chain B residue 256 type sequence D description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 16) chain B residue 258 type sequence K description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 17) chain B residue 291 type sequence G description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 18) chain B residue 292 type sequence T description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 19) chain B residue 217 type sequence E description BINDING SITE FOR RESIDUE ACT B 1393 source : BC1 20) chain B residue 220 type sequence K description BINDING SITE FOR RESIDUE ACT B 1393 source : BC1 21) chain B residue 279 type sequence V description BINDING SITE FOR RESIDUE ACT B 1393 source : BC1 22) chain B residue 170 type sequence E description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 23) chain B residue 173 type sequence G description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 24) chain B residue 175 type sequence E description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 25) chain B residue 176 type sequence H description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 26) chain B residue 201 type sequence H description BINDING SITE FOR RESIDUE EDO B 1396 source : BC4 27) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE EDO B 1397 source : BC5 28) chain B residue 203 type sequence A description BINDING SITE FOR RESIDUE EDO B 1397 source : BC5 29) chain B residue 204 type sequence T description BINDING SITE FOR RESIDUE EDO B 1397 source : BC5 30) chain B residue 280 type sequence H description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 31) chain B residue 281 type sequence A description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 32) chain B residue 287 type sequence X description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 33) chain B residue 136 type sequence G description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 34) chain B residue 137 type sequence R description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 35) chain B residue 229 type sequence D description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 36) chain B residue 231 type sequence Q description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 37) chain B residue 248 type sequence H description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 38) chain B residue 309 type sequence K description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 39) chain B residue 373 type sequence M description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 40) chain B residue 374 type sequence L description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 41) chain B residue 171 type sequence K description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 42) chain B residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 258 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 44) chain B residue 288 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 256 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 47) chain B residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 48) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 49) chain B residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 50) chain B residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 51) chain B residue 287 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3

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