eF-site ID 2wtv-ABCD PDB Code 2wtv Chain A, B, C, D click to enlarge Title Aurora-A Inhibitor Structure Classification TRANSFERASE Compound SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1 Source Homo sapiens (Human) (STK6_HUMAN) Sequence A:  KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVL FKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDAT RVYLILEYAPRGEVYKELQKLSKFDEQRTATYITELANAL SYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS RRXXLXGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV GKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLL KHNPSQRPMLREVLEHPWITANSSK B:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPRGEVYKELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR RXXLXGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK HNPSQRPMLREVLEHPWITANSSK C:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR VYLILEYAPRGEVYKELQKLSKFDEQRTATYITELANALS YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR RXXLXGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK HNPSQRPMLREVLEHPWITANSSK D:  KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVL FKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDAT RVYLILEYAPRGEVYKELQKLSKFDEQRTATYITELANAL SYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS RRXXLXGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV GKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLL KHNPSQRPMLREVLEHPWITANSSK Description Functional site 1) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 2) chain A residue 147 type sequence V description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 3) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 4) chain A residue 194 type sequence L description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 5) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 6) chain A residue 212 type sequence Y description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 7) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 8) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 9) chain A residue 263 type sequence L description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 10) chain A residue 273 type sequence A description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 11) chain A residue 274 type sequence D description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 12) chain A residue 279 type sequence V description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 13) chain C residue 171 type sequence K description BINDING SITE FOR RESIDUE ZZL A 1390 source : AC1 14) chain A residue 231 type sequence Q description BINDING SITE FOR RESIDUE EDO A 1391 source : AC2 15) chain A residue 385 type sequence A description BINDING SITE FOR RESIDUE EDO A 1391 source : AC2 16) chain A residue 386 type sequence N description BINDING SITE FOR RESIDUE EDO A 1391 source : AC2 17) chain A residue 387 type sequence S description BINDING SITE FOR RESIDUE EDO A 1391 source : AC2 18) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE ACT A 1392 source : AC3 19) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE ACT A 1392 source : AC3 20) chain A residue 279 type sequence V description BINDING SITE FOR RESIDUE ACT A 1392 source : AC3 21) chain A residue 248 type sequence H description BINDING SITE FOR RESIDUE ACT A 1393 source : AC4 22) chain A residue 373 type sequence M description BINDING SITE FOR RESIDUE ACT A 1393 source : AC4 23) chain A residue 374 type sequence L description BINDING SITE FOR RESIDUE ACT A 1393 source : AC4 24) chain A residue 148 type sequence Y description BINDING SITE FOR RESIDUE DMS A 1394 source : AC5 25) chain A residue 205 type sequence R description BINDING SITE FOR RESIDUE DMS A 1394 source : AC5 26) chain C residue 138 type sequence P description BINDING SITE FOR RESIDUE DMS A 1394 source : AC5 27) chain A residue 146 type sequence N description BINDING SITE FOR RESIDUE EDO C 1390 source : AC6 28) chain A residue 148 type sequence Y description BINDING SITE FOR RESIDUE EDO C 1390 source : AC6 29) chain C residue 136 type sequence G description BINDING SITE FOR RESIDUE EDO C 1390 source : AC6 30) chain C residue 137 type sequence R description BINDING SITE FOR RESIDUE EDO C 1390 source : AC6 31) chain B residue 139 type sequence L description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 32) chain B residue 141 type sequence K description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 33) chain B residue 147 type sequence V description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 34) chain B residue 162 type sequence K description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 35) chain B residue 194 type sequence L description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 36) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 37) chain B residue 212 type sequence Y description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 38) chain B residue 213 type sequence A description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 39) chain B residue 261 type sequence N description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 40) chain B residue 263 type sequence L description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 41) chain B residue 273 type sequence A description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 42) chain B residue 274 type sequence D description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 43) chain B residue 275 type sequence F description BINDING SITE FOR RESIDUE ZZL B 1390 source : AC7 44) chain B residue 138 type sequence P description BINDING SITE FOR RESIDUE DMS B 1391 source : AC8 45) chain D residue 148 type sequence Y description BINDING SITE FOR RESIDUE DMS B 1391 source : AC8 46) chain D residue 205 type sequence R description BINDING SITE FOR RESIDUE DMS B 1391 source : AC8 47) chain B residue 256 type sequence D description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 48) chain B residue 258 type sequence K description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 49) chain B residue 291 type sequence G description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 50) chain B residue 292 type sequence T description BINDING SITE FOR RESIDUE ACT B 1392 source : AC9 51) chain B residue 217 type sequence E description BINDING SITE FOR RESIDUE ACT B 1393 source : BC1 52) chain B residue 220 type sequence K description BINDING SITE FOR RESIDUE ACT B 1393 source : BC1 53) chain B residue 279 type sequence V description BINDING SITE FOR RESIDUE ACT B 1393 source : BC1 54) chain D residue 146 type sequence N description BINDING SITE FOR RESIDUE EDO B 1394 source : BC2 55) chain B residue 170 type sequence E description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 56) chain B residue 173 type sequence G description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 57) chain B residue 175 type sequence E description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 58) chain B residue 176 type sequence H description BINDING SITE FOR RESIDUE EDO B 1395 source : BC3 59) chain B residue 201 type sequence H description BINDING SITE FOR RESIDUE EDO B 1396 source : BC4 60) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE EDO B 1397 source : BC5 61) chain B residue 203 type sequence A description BINDING SITE FOR RESIDUE EDO B 1397 source : BC5 62) chain B residue 204 type sequence T description BINDING SITE FOR RESIDUE EDO B 1397 source : BC5 63) chain B residue 280 type sequence H description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 64) chain B residue 281 type sequence A description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 65) chain B residue 287 type sequence X description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 66) chain D residue 266 type sequence S description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 67) chain D residue 269 type sequence E description BINDING SITE FOR RESIDUE EDO B 1398 source : BC6 68) chain B residue 136 type sequence G description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 69) chain B residue 137 type sequence R description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 70) chain D residue 146 type sequence N description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 71) chain D residue 148 type sequence Y description BINDING SITE FOR RESIDUE EDO B 1399 source : BC7 72) chain B residue 229 type sequence D description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 73) chain B residue 231 type sequence Q description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 74) chain C residue 229 type sequence D description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 75) chain C residue 231 type sequence Q description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 76) chain C residue 232 type sequence R description BINDING SITE FOR RESIDUE EDO C 1391 source : BC8 77) chain B residue 248 type sequence H description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 78) chain B residue 309 type sequence K description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 79) chain B residue 373 type sequence M description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 80) chain B residue 374 type sequence L description BINDING SITE FOR RESIDUE ACT B 1400 source : BC9 81) chain C residue 139 type sequence L description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 82) chain C residue 141 type sequence K description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 83) chain C residue 147 type sequence V description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 84) chain C residue 162 type sequence K description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 85) chain C residue 194 type sequence L description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 86) chain C residue 211 type sequence E description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 87) chain C residue 212 type sequence Y description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 88) chain C residue 213 type sequence A description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 89) chain C residue 261 type sequence N description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 90) chain C residue 263 type sequence L description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 91) chain C residue 273 type sequence A description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 92) chain C residue 274 type sequence D description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 93) chain C residue 275 type sequence F description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 94) chain C residue 279 type sequence V description BINDING SITE FOR RESIDUE ZZL C 1392 source : CC1 95) chain C residue 248 type sequence H description BINDING SITE FOR RESIDUE ACT C 1393 source : CC2 96) chain C residue 309 type sequence K description BINDING SITE FOR RESIDUE ACT C 1393 source : CC2 97) chain C residue 373 type sequence M description BINDING SITE FOR RESIDUE ACT C 1393 source : CC2 98) chain C residue 374 type sequence L description BINDING SITE FOR RESIDUE ACT C 1393 source : CC2 99) chain C residue 217 type sequence E description BINDING SITE FOR RESIDUE ACT C 1394 source : CC3 100) chain C residue 220 type sequence K description BINDING SITE FOR RESIDUE ACT C 1394 source : CC3 101) chain C residue 256 type sequence D description BINDING SITE FOR RESIDUE EDO C 1395 source : CC4 102) chain C residue 258 type sequence K description BINDING SITE FOR RESIDUE EDO C 1395 source : CC4 103) chain C residue 291 type sequence G description BINDING SITE FOR RESIDUE EDO C 1395 source : CC4 104) chain C residue 292 type sequence T description BINDING SITE FOR RESIDUE EDO C 1395 source : CC4 105) chain B residue 171 type sequence K description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 106) chain D residue 140 type sequence G description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 107) chain D residue 147 type sequence V description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 108) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 109) chain D residue 194 type sequence L description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 110) chain D residue 211 type sequence E description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 111) chain D residue 212 type sequence Y description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 112) chain D residue 213 type sequence A description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 113) chain D residue 261 type sequence N description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 114) chain D residue 263 type sequence L description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 115) chain D residue 273 type sequence A description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 116) chain D residue 274 type sequence D description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 117) chain D residue 279 type sequence V description BINDING SITE FOR RESIDUE ZZL D 1390 source : CC5 118) chain D residue 346 type sequence F description BINDING SITE FOR RESIDUE EDO D 1391 source : CC6 119) chain D residue 348 type sequence F description BINDING SITE FOR RESIDUE EDO D 1391 source : CC6 120) chain D residue 217 type sequence E description BINDING SITE FOR RESIDUE ACT D 1392 source : CC7 121) chain D residue 260 type sequence E description BINDING SITE FOR RESIDUE ACT D 1392 source : CC7 122) chain D residue 279 type sequence V description BINDING SITE FOR RESIDUE ACT D 1392 source : CC7 123) chain D residue 248 type sequence H description BINDING SITE FOR RESIDUE ACT D 1393 source : CC8 124) chain D residue 309 type sequence K description BINDING SITE FOR RESIDUE ACT D 1393 source : CC8 125) chain D residue 374 type sequence L description BINDING SITE FOR RESIDUE ACT D 1393 source : CC8 126) 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 127) 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 128) 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 129) 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 130) chain A residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 131) chain A residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 132) chain A residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 133) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 134) chain C residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 135) chain C residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 136) chain C residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 137) chain C residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 138) chain C residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 139) chain D residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 140) chain D residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 141) chain D residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 142) chain D residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 143) chain D residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 144) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 145) chain B residue 143 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 146) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 147) chain B residue 211 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 148) chain B residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 149) chain A residue 260 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X source Swiss-Prot : SWS_FT_FI2 150) chain A residue 287 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 151) chain B residue 287 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 152) chain C residue 287 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 153) chain D residue 287 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 source Swiss-Prot : SWS_FT_FI3 154) 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 155) 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 156) 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 157) 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 158) chain A residue 139-162 type prosite sequence LGKGKFGNVYLAREKQSKFILALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK source prosite : PS00107 159) chain A residue 252-264 type prosite sequence VIHRDIKPENLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL source prosite : PS00108 160) chain A residue 288 type MOD_RES sequence X 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 161) chain B residue 288 type MOD_RES sequence X 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 162) chain C residue 288 type MOD_RES sequence X 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 163) chain D residue 288 type MOD_RES sequence X 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 164) 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 165) 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 166) 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 167) 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

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