eF-site ID 2c6e-B PDB Code 2c6e Chain B 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 B:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADGTLDYLPPEMIE GRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRIS RVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPW ITANSS Description Functional site 1) chain B residue 136 type sequence R description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 2) chain B residue 138 type sequence L description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 3) chain B residue 161 type sequence K description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 4) chain B residue 177 type sequence L description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 5) chain B residue 184 type sequence Q description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 6) chain B residue 193 type sequence L description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 7) chain B residue 207 type sequence L description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 8) chain B residue 210 type sequence E description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 9) chain B residue 211 type sequence Y description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 10) chain B residue 212 type sequence A description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 11) chain B residue 213 type sequence P description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 12) chain B residue 215 type sequence G description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 13) chain B residue 262 type sequence L description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 14) chain B residue 273 type sequence D description BINDING SITE FOR RESIDUE HPM B1388 source : AC2 15) chain B 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 16) chain B residue 273 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 17) chain B residue 142 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 18) chain B residue 161 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 19) chain B residue 210 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 20) chain B residue 259 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 21) chain B residue 341 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 22) chain B 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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