eF-site ID 1ol5-AB PDB Code 1ol5 Chain A, B click to enlarge Title Structure of Aurora-A 122-403, phosphorylated on Thr287, Thr288 and bound to TPX2 1-43 Classification TRANSFERASE/CELL CYCLE Compound SERINE/THREONINE KINASE 6 Source null (DIL2_HUMAN) Sequence A:  SKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALK VLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHD ATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELAN ALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAP SSRRXXLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEF LVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISR LLKHNPSQRPMLREVLEHPWITANSS B:  SYSYDAPSDFINFSSLNIDSWFEEKANLEN Description (1)  SERINE/THREONINE KINASE 6 (E.C.2.7.1.37), RESTRICTED EXPRESSION PROLIFERATION ASSOCIATED PROTEIN 100 Functional site 1) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE MG A1389 source : AC1 2) chain A residue 274 type sequence D description BINDING SITE FOR RESIDUE MG A1389 source : AC1 3) chain A residue 245 type sequence S description BINDING SITE FOR RESIDUE SO4 A1391 source : AC3 4) chain A residue 373 type sequence M description BINDING SITE FOR RESIDUE SO4 A1391 source : AC3 5) chain A residue 374 type sequence L description BINDING SITE FOR RESIDUE SO4 A1391 source : AC3 6) chain A residue 375 type sequence R description BINDING SITE FOR RESIDUE SO4 A1391 source : AC3 7) chain A residue 220 type sequence R description BINDING SITE FOR RESIDUE SO4 A1392 source : AC4 8) chain A residue 224 type sequence K description BINDING SITE FOR RESIDUE SO4 A1392 source : AC4 9) chain A residue 176 type sequence H description BINDING SITE FOR RESIDUE SO4 A1393 source : AC5 10) chain A residue 180 type sequence R description BINDING SITE FOR RESIDUE SO4 A1393 source : AC5 11) chain A residue 286 type sequence R description BINDING SITE FOR RESIDUE SO4 A1393 source : AC5 12) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 13) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 14) chain A residue 147 type sequence V description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 15) chain A residue 160 type sequence A description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 16) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 17) chain A residue 194 type sequence L description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 18) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 19) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 20) chain A residue 217 type sequence T description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 21) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 22) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 23) chain A residue 263 type sequence L description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 24) chain A residue 274 type sequence D description BINDING SITE FOR RESIDUE ADP A1388 source : AC7 25) chain A 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 26) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 27) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 28) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 29) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 30) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 31) chain A residue 287 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 32) chain A 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 33) chain A residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 34) chain A 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 35) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 36) chain A residue 252-264 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108

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