eF-site ID 2bmc-D PDB Code 2bmc Chain D click to enlarge Title Aurora-2 T287D T288D complexed with PHA-680632 Classification TRANSFERASE Compound SERINE THREONINE-PROTEIN KINASE 6 Source (STK6_HUMAN) Sequence D:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSKPSNCQ Description (1)  SERINE THREONINE-PROTEIN KINASE 6 (E.C.2.7.1.37) Functional site 1) chain D residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 2) chain D residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 3) chain D residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 4) chain D residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 5) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 6) chain D residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 7) chain D residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 8) chain D residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 9) chain D residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 10) chain D residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 11) chain D residue 217 type sequence T description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 12) chain D residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 13) chain D residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 14) chain D residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 15) 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 16) 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 17) chain D residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 18) chain D residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 19) chain D residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 20) chain D residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 21) chain D residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 22) 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

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