eF-site ID 2j50-AB PDB Code 2j50 Chain A, B click to enlarge Title Structure of Aurora-2 in complex with PHA-739358 Classification TRANSFERASE Compound SERINE/THREONINE-PROTEIN KINASE 6 Source (STK6_HUMAN) Sequence A:  WALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKA QLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVY LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYC HSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLCGTLDY LPPEMIEDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYK RISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLE HPWITANSSK B:  WALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKA QLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVY LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYC HSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLCGTLDY LPPEMIEDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYK RISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLE HPWITANSSK Description (1)  SERINE/THREONINE-PROTEIN KINASE 6 (E.C.2.7.11.1) Functional site 1) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1391 source : AC1 2) chain A residue 143 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1391 source : AC1 3) chain A residue 144 type sequence F description BINDING SITE FOR RESIDUE SO4 A 1391 source : AC1 4) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1391 source : AC1 5) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1391 source : AC2 6) chain B residue 143 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1391 source : AC2 7) chain B residue 144 type sequence F description BINDING SITE FOR RESIDUE SO4 B 1391 source : AC2 8) chain B residue 162 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1391 source : AC2 9) chain A residue 160 type sequence A description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 10) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 11) chain A residue 194 type sequence L description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 12) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 13) chain A residue 212 type sequence Y description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 14) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 15) chain A residue 214 type sequence P description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 16) chain A residue 215 type sequence L description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 17) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 18) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 19) chain A residue 275 type sequence F description BINDING SITE FOR RESIDUE 627 A 1390 source : AC3 20) chain B residue 160 type sequence A description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 21) chain B residue 162 type sequence K description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 22) chain B residue 194 type sequence L description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 23) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 24) chain B residue 212 type sequence Y description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 25) chain B residue 213 type sequence A description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 26) chain B residue 214 type sequence P description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 27) chain B residue 215 type sequence L description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 28) chain B residue 216 type sequence G description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 29) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 30) chain B residue 275 type sequence F description BINDING SITE FOR RESIDUE 627 B 1390 source : AC4 31) 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 32) 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 33) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 34) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 35) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 36) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 37) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 38) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 39) chain B residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 40) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 41) chain B residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 42) chain B residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 43) chain A residue 288 type MOD_RES sequence T 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 44) chain B residue 288 type MOD_RES sequence T 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 A residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 46) 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 47) 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 48) 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 49) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 50) 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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