eF-site ID 2bmc-F PDB Code 2bmc Chain F click to enlarge Title Aurora-2 T287D T288D complexed with PHA-680632 Classification TRANSFERASE Compound SERINE THREONINE-PROTEIN KINASE 6 Source (STK6_HUMAN) Sequence F:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLP PEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQET YKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREV LEHPWITANSSKPSNCQ Description Functional site 1) chain F residue 139 type sequence L description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 2) chain F residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 3) chain F residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 4) chain F residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 5) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 6) chain F residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 7) chain F residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 8) chain F residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 9) chain F residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 10) chain F residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 11) chain F residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 12) chain F residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 13) chain F 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 14) chain F residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 15) chain F residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 16) chain F residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 17) chain F residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 18) chain F residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 19) chain F residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 20) chain F 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

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