eF-site ID 2j4z-AB PDB Code 2j4z Chain A, B click to enlarge Title Structure of Aurora-2 in complex with PHA-680626 Classification TRANSFERASE Compound SERINE THREONINE-PROTEIN KINASE 6 Source (STK6_HUMAN) Sequence A:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK HNPSQRPMLREVLEHPWITANSSK B:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK HNPSQRPMLREVLEHPWITANSSKPSNCQN Description Functional site 1) chain A residue 160 type sequence A description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 2) chain A residue 194 type sequence L description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 3) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 4) chain A residue 212 type sequence Y description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 5) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 6) chain A residue 214 type sequence P description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 7) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 8) chain A residue 220 type sequence R description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 9) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 10) chain A residue 263 type sequence L description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 11) chain A residue 273 type sequence A description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 12) chain A residue 280 type sequence H description BINDING SITE FOR RESIDUE 626 A 1389 source : AC1 13) chain A residue 247 type sequence C description BINDING SITE FOR RESIDUE ARS A 1390 source : AC2 14) chain A residue 255 type sequence R description BINDING SITE FOR RESIDUE ARS A 1390 source : AC2 15) chain A residue 290 type sequence C description BINDING SITE FOR RESIDUE ARS A 1391 source : AC3 16) chain A residue 385 type sequence A description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 17) chain B residue 160 type sequence A description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 18) chain B residue 194 type sequence L description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 19) chain B residue 210 type sequence L description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 20) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 21) chain B residue 212 type sequence Y description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 22) chain B residue 213 type sequence A description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 23) chain B residue 214 type sequence P description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 24) chain B residue 216 type sequence G description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 25) chain B residue 220 type sequence R description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 26) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 27) chain B residue 263 type sequence L description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 28) chain B residue 273 type sequence A description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 29) chain B residue 280 type sequence H description BINDING SITE FOR RESIDUE 626 B 1395 source : AC4 30) chain B residue 247 type sequence C description BINDING SITE FOR RESIDUE ARS B 1396 source : AC5 31) chain B residue 255 type sequence R description BINDING SITE FOR RESIDUE ARS B 1396 source : AC5 32) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 33) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 34) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 35) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 36) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 37) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 38) chain B residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 39) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 40) chain B residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 41) chain B residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 42) chain A residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 288 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 288 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606 source Swiss-Prot : SWS_FT_FI4 46) 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 47) 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 48) 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 49) 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 50) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 51) chain A residue 252-264 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108 52) 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 53) 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

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