eF-site ID 1oiu-ABCD PDB Code 1oiu Chain A, B, C, D click to enlarge Title Structure of human Thr160-phospho CDK2/cyclin A complexed with a 6-cyclohexylmethyloxy-2-anilino-purine inhibitor Classification KINASE Compound CELL DIVISION PROTEIN KINASE 2 Source null (CGA2_HUMAN) Sequence A:  PGSMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRL TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHLR B:  DYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVD WLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLV GTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEH LVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFL GELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESL IRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNS KYHGVSLLNPPETLNL C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGVPPLDEDGRSLLSQMLHYD PNKRISAKAALAHPFFQDVTKPVPHL D:  DYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVD WLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLV GTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEH LVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFL GELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESL IRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNS KYHGVSLLNPPETLNL Description Functional site 1) chain B residue 200 type sequence M description BINDING SITE FOR RESIDUE MG B1433 source : AC1 2) chain B residue 203 type sequence Q description BINDING SITE FOR RESIDUE MG B1433 source : AC1 3) chain B residue 206 type sequence I description BINDING SITE FOR RESIDUE MG B1433 source : AC1 4) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 5) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 6) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 7) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 8) chain A residue 64 type sequence V description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 9) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 10) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 11) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 12) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 13) chain A residue 84 type sequence H description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 14) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 15) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE N76 A1298 source : AC2 16) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 17) chain C residue 12 type sequence E description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 18) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 19) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 20) chain C residue 64 type sequence V description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 21) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 22) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 23) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 24) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 25) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 26) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 27) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 28) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 29) chain B residue 189 type sequence M description BINDING SITE FOR RESIDUE SGM B1193 source : AC4 30) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE SGM B1193 source : AC4 31) chain B residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM B1193 source : AC4 32) chain B residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM B1193 source : AC4 33) chain B residue 305 type sequence D description BINDING SITE FOR RESIDUE SGM B1193 source : AC4 34) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE SGM D1193 source : AC5 35) chain D residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM D1193 source : AC5 36) chain D residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM D1193 source : AC5 37) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 38) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 39) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 41) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 42) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 44) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 45) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 46) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 47) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 48) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 49) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 50) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 14 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 source Swiss-Prot : SWS_FT_FI7 52) chain C residue 14 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 source Swiss-Prot : SWS_FT_FI7 53) chain A residue 15 type MOD_RES sequence Y description Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 54) chain C residue 15 type MOD_RES sequence Y description Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 55) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 56) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 57) chain A residue 160 type MOD_RES sequence X description Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995 source Swiss-Prot : SWS_FT_FI10 58) chain C residue 160 type MOD_RES sequence X description Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995 source Swiss-Prot : SWS_FT_FI10 59) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 60) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 61) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 62) chain A residue 10 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 33 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 64) chain C residue 129 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 65) chain A residue 81 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 66) chain A residue 86 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 129 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 68) chain C residue 10 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 69) chain C residue 33 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 81 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 86 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 72) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 73) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

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