eF-site ID 2c6e-A PDB Code 2c6e Chain A click to enlarge Title Aurora A kinase activated mutant (T287D) in complex with a 5- aminopyrimidinyl quinazoline inhibitor Classification TRANSFERASE/INHIBITOR Compound SERINE/THREONINE-PROTEIN KINASE 6 Source Homo sapiens (Human) (STK6_HUMAN) Sequence A:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSGTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSK Description Functional site 1) chain A residue 136 type sequence R description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 2) chain A residue 138 type sequence L description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 3) chain A residue 161 type sequence K description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 4) chain A residue 184 type sequence Q description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 5) chain A residue 193 type sequence L description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 6) chain A residue 209 type sequence L description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 7) chain A residue 210 type sequence E description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 8) chain A residue 211 type sequence Y description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 9) chain A residue 212 type sequence A description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 10) chain A residue 213 type sequence P description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 11) chain A residue 215 type sequence G description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 12) chain A residue 216 type sequence T description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 13) chain A residue 262 type sequence L description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 14) chain A residue 273 type sequence D description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 15) chain A residue 274 type sequence F description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 16) chain A residue 276 type sequence W description BINDING SITE FOR RESIDUE HPM A1389 source : AC1 17) chain A residue 138-161 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 18) chain A residue 251-263 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108 19) chain A residue 255 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 20) chain A residue 142 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 21) chain A residue 161 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 22) chain A residue 210 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 23) chain A residue 259 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 24) chain A residue 273 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 25) chain A residue 341 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 257 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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