eF-site ID 2bmc-A PDB Code 2bmc Chain A click to enlarge Title Aurora-2 T287D T288D complexed with PHA-680632 Classification TRANSFERASE Compound SERINE THREONINE-PROTEIN KINASE 6 Source (STK6_HUMAN) Sequence A:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSKPSNCQ Description (1)  SERINE THREONINE-PROTEIN KINASE 6 (E.C.2.7.1.37) Functional site 1) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 2) chain A residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 3) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 4) chain A residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 5) chain A residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 6) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 7) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 8) chain A residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 9) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 10) chain A residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 11) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 12) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 13) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 14) chain A residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 15) 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 16) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 17) chain A residue 252-264 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108 18) 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 19) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 20) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 21) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 22) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 23) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 24) 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

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