eF-site ID 2bmc-ABCDEF PDB Code 2bmc Chain A, B, C, D, E, 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 A:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSKPSNCQ B:  KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVL FKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDAT RVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANAL SYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYL PPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQE TYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLRE VLEHPWITANSSKPSNCQ C:  KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVL FKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDAT RVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANAL SYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYL PPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQE TYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLRE VLEHPWITANSSKPSNC D:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSKPSNCQ E:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLPP EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVL EHPWITANSSKPSNCQ F:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLDYLP PEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQET YKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREV LEHPWITANSSKPSNCQ Description (1)  SERINE THREONINE-PROTEIN KINASE 6 (E.C.2.7.1.37) Functional site 1) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 2) chain A residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 3) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 4) chain A residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 5) chain A residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 6) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 7) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 8) chain A residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 9) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 10) chain A residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 11) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 12) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 13) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 14) chain A residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 15) chain B residue 266 type sequence S description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 16) chain B residue 267 type sequence A description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 17) chain B residue 268 type sequence G description BINDING SITE FOR RESIDUE MPY A1395 source : AC1 18) chain B residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 19) chain B residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 20) chain B residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 21) chain B residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 22) chain B residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 23) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 24) chain B residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 25) chain B residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 26) chain B residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 27) chain B residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 28) chain B residue 224 type sequence K description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 29) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 30) chain B residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 31) chain B residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY B1395 source : AC2 32) chain C residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 33) chain C residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 34) chain C residue 142 type sequence G description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 35) chain C residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 36) chain C residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 37) chain C residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 38) chain C residue 194 type sequence L description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 39) chain C residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 40) chain C residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 41) chain C residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 42) chain C residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 43) chain C residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 44) chain C residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 45) chain C residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 46) chain C residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY C1394 source : AC3 47) chain C residue 215 type sequence L description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 48) chain D residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 49) chain D residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 50) chain D residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 51) chain D residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 52) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 53) chain D residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 54) chain D residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 55) chain D residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 56) chain D residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 57) chain D residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 58) chain D residue 217 type sequence T description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 59) chain D residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 60) chain D residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 61) chain D residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY D1395 source : AC4 62) chain E residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 63) chain E residue 141 type sequence K description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 64) chain E residue 142 type sequence G description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 65) chain E residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 66) chain E residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 67) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 68) chain E residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 69) chain E residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 70) chain E residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 71) chain E residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 72) chain E residue 216 type sequence G description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 73) chain E residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 74) chain E residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 75) chain E residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY E1395 source : AC5 76) chain E residue 266 type sequence S description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 77) chain F residue 139 type sequence L description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 78) chain F residue 140 type sequence G description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 79) chain F residue 147 type sequence V description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 80) chain F residue 160 type sequence A description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 81) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 82) chain F residue 211 type sequence E description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 83) chain F residue 212 type sequence Y description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 84) chain F residue 213 type sequence A description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 85) chain F residue 214 type sequence P description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 86) chain F residue 260 type sequence E description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 87) chain F residue 261 type sequence N description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 88) chain F residue 263 type sequence L description BINDING SITE FOR RESIDUE MPY F1395 source : AC6 89) chain A 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 90) 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 91) chain B 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 92) chain C 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 93) 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 94) 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 95) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 96) chain A residue 252-264 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108 97) chain A 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 98) chain B 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 99) chain C 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 100) 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 101) 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 102) 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 103) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 104) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 105) chain C residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 106) chain C residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 107) chain C residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 108) chain C residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 109) chain C residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 110) chain D residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 111) chain D residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 112) chain D residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 113) chain D residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 114) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 115) chain D residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 116) chain E residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 117) chain E residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 118) chain E residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 119) chain E residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 120) chain E residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 121) chain F residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 122) chain F residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 123) chain F residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 124) chain F residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 125) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 126) chain F residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 127) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 128) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 129) chain B residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 130) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 131) chain B residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 132) chain B residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 133) chain A residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 134) chain B residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 135) chain C residue 342 type MOD_RES sequence S description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 source Swiss-Prot : SWS_FT_FI5 136) 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 137) 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 138) 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

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