eF-site ID 3uol-AB PDB Code 3uol Chain A, B click to enlarge Title Aurora A in complex with SO2-162 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Aurora kinase A Source Homo sapiens (Human) (AURKA_HUMAN) Sequence A:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRR DTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGK PPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKH NPSQRPMLREVLEHPWITANSSK B:  QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFK AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSY CHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRR DTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGK PPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKH NPSQRPMLREVLEHPWITANSSK Description Functional site 1) chain A residue 137 type sequence R description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 2) chain A residue 139 type sequence L description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 3) chain A residue 194 type sequence L description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 4) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 5) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 6) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 7) chain A residue 217 type sequence T description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 8) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 9) chain A residue 263 type sequence L description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 10) chain A residue 273 type sequence A description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 11) chain A residue 279 type sequence V description BINDING SITE FOR RESIDUE 0C7 A 2 source : AC1 12) chain A residue 366 type sequence H description BINDING SITE FOR RESIDUE EDO A 1 source : AC2 13) chain A residue 367 type sequence N description BINDING SITE FOR RESIDUE EDO A 1 source : AC2 14) chain A residue 302 type sequence E description BINDING SITE FOR RESIDUE EDO A 4 source : AC3 15) chain A residue 342 type sequence S description BINDING SITE FOR RESIDUE EDO A 4 source : AC3 16) chain A residue 343 type sequence R description BINDING SITE FOR RESIDUE EDO A 4 source : AC3 17) chain A residue 366 type sequence H description BINDING SITE FOR RESIDUE EDO A 4 source : AC3 18) chain B residue 335 type sequence Q description BINDING SITE FOR RESIDUE EDO A 4 source : AC3 19) chain A residue 130 type sequence L description BINDING SITE FOR RESIDUE EDO A 6 source : AC4 20) chain A residue 148 type sequence Y description BINDING SITE FOR RESIDUE EDO A 6 source : AC4 21) chain A residue 205 type sequence R description BINDING SITE FOR RESIDUE EDO A 6 source : AC4 22) chain A residue 227 type sequence K description BINDING SITE FOR RESIDUE EDO A 7 source : AC5 23) chain A residue 350 type sequence D description BINDING SITE FOR RESIDUE EDO A 10 source : AC6 24) chain A residue 351 type sequence F description BINDING SITE FOR RESIDUE EDO A 10 source : AC6 25) chain B residue 137 type sequence R description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 26) chain B residue 139 type sequence L description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 27) chain B residue 194 type sequence L description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 28) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 29) chain B residue 213 type sequence A description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 30) chain B residue 216 type sequence G description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 31) chain B residue 217 type sequence T description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 32) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 33) chain B residue 263 type sequence L description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 34) chain B residue 273 type sequence A description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 35) chain B residue 279 type sequence V description BINDING SITE FOR RESIDUE 0C7 B 1 source : AC7 36) chain B residue 199 type sequence Y description BINDING SITE FOR RESIDUE EDO B 2 source : AC8 37) chain B residue 200 type sequence F description BINDING SITE FOR RESIDUE EDO B 2 source : AC8 38) chain B residue 201 type sequence H description BINDING SITE FOR RESIDUE EDO B 2 source : AC8 39) chain B residue 366 type sequence H description BINDING SITE FOR RESIDUE EDO B 3 source : AC9 40) chain B residue 367 type sequence N description BINDING SITE FOR RESIDUE EDO B 3 source : AC9 41) chain B residue 130 type sequence L description BINDING SITE FOR RESIDUE EDO B 5 source : BC1 42) chain B residue 148 type sequence Y description BINDING SITE FOR RESIDUE EDO B 5 source : BC1 43) chain B residue 205 type sequence R description BINDING SITE FOR RESIDUE EDO B 5 source : BC1 44) chain B residue 227 type sequence K description BINDING SITE FOR RESIDUE EDO B 8 source : BC2 45) chain B residue 350 type sequence D description BINDING SITE FOR RESIDUE EDO B 9 source : BC3 46) chain B residue 351 type sequence F description BINDING SITE FOR RESIDUE EDO B 9 source : BC3 47) chain B residue 248 type sequence H description BINDING SITE FOR RESIDUE EDO B 11 source : BC4 48) chain B residue 308 type sequence E description BINDING SITE FOR RESIDUE EDO B 11 source : BC4 49) chain B residue 373 type sequence M description BINDING SITE FOR RESIDUE EDO B 11 source : BC4 50) chain B residue 374 type sequence L description BINDING SITE FOR RESIDUE EDO B 11 source : BC4 51) 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 52) 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 53) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 54) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 55) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 56) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 57) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 58) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 59) chain B residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 60) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 61) chain B residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 62) chain B residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 63) chain A residue 287 type MOD_RES sequence D description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 64) chain B residue 287 type MOD_RES sequence D description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 72) chain A residue 252-264 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108

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