eF-site ID 2bmc-E PDB Code 2bmc Chain E click to enlarge Title Aurora-2 T287D T288D complexed with PHA-680632 Classification TRANSFERASE Compound SERINE THREONINE-PROTEIN KINASE 6 Source (STK6_HUMAN) Sequence E:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSKPSNCQ Description (1)  SERINE THREONINE-PROTEIN KINASE 6 (E.C.2.7.1.37) Functional site 1) chain E residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 2) chain E residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 3) chain E residue 142 type sequence G description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 4) chain E residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 5) chain E residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 6) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 7) chain E residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 8) chain E residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 9) chain E residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 10) chain E residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 11) chain E residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 12) chain E residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 13) chain E residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 14) chain E residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 15) chain E residue 266 type sequence S description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 16) chain E 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 17) chain E 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 18) chain E residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 19) chain E residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 20) chain E residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 21) chain E residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 22) chain E residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 23) chain E 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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