eF-site ID 2wtv-D PDB Code 2wtv Chain D 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 D:  KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVL FKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDAT RVYLILEYAPRGEVYKELQKLSKFDEQRTATYITELANAL SYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS RRXXLXGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV GKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLL KHNPSQRPMLREVLEHPWITANSSK Description Functional site 1) chain D residue 148 type sequence Y description BINDING SITE FOR RESIDUE DMS B 1391 source : AC8 2) chain D residue 205 type sequence R description BINDING SITE FOR RESIDUE DMS B 1391 source : AC8 3) chain D residue 146 type sequence N description BINDING SITE FOR RESIDUE EDO B 1394 source : BC2 4) chain D residue 266 type sequence S description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 5) chain D residue 269 type sequence E description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 6) chain D residue 146 type sequence N description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 7) chain D residue 148 type sequence Y description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 8) chain D residue 140 type sequence G description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 9) chain D residue 147 type sequence V description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 10) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 11) chain D residue 194 type sequence L description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 12) chain D residue 211 type sequence E description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 13) chain D residue 212 type sequence Y description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 14) chain D residue 213 type sequence A description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 15) chain D residue 261 type sequence N description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 16) chain D residue 263 type sequence L description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 17) chain D residue 273 type sequence A description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 18) chain D residue 274 type sequence D description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 19) chain D residue 279 type sequence V description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 20) chain D residue 346 type sequence F description BINDING SITE FOR RESIDUE EDO D 1391 source : CC6 21) chain D residue 348 type sequence F description BINDING SITE FOR RESIDUE EDO D 1391 source : CC6 22) chain D residue 217 type sequence E description BINDING SITE FOR RESIDUE ACT D 1392 source : CC7 23) chain D residue 260 type sequence E description BINDING SITE FOR RESIDUE ACT D 1392 source : CC7 24) chain D residue 279 type sequence V description BINDING SITE FOR RESIDUE ACT D 1392 source : CC7 25) chain D residue 248 type sequence H description BINDING SITE FOR RESIDUE ACT D 1393 source : CC8 26) chain D residue 309 type sequence K description BINDING SITE FOR RESIDUE ACT D 1393 source : CC8 27) chain D residue 374 type sequence L description BINDING SITE FOR RESIDUE ACT D 1393 source : CC8 28) chain D residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 29) chain D 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 30) chain D 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 31) chain D 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 32) chain D residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 33) chain D residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 34) chain D residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 35) chain D residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 36) chain D residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 37) chain D 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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