eF-site ID 4bcp-ABCD PDB Code 4bcp Chain A, B, C, D click to enlarge Title Structure of CDK2 in complex with cyclin A and a 2-amino-4-heteroaryl- pyrimidine inhibitor Classification TRANSFERASE/CELL CYCLE Compound CYCLIN-DEPENDENT KINASE 2 Source Homo sapiens (Human) (CCNA2_HUMAN) Sequence A:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKA ALAHPFFQDVTKPVPHLRL B:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF LGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPES LIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN SKYHGVSLLNPPETLNL C:  SMENFQKVEKIGEGVVYKARNKLTGEVVALKKIRLDTETE GVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF LHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHR VLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYXHE VVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRAL FPGDSEIDQLFRIFRTLGTFSKVVPPLDEDGRSLLSQMLH YDPNKRISAKAALAHPFFQDVTKPVPHL D:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF LGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPES LIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN SKYHGVSLLNPPETLNL Description (1)  CYCLIN-DEPENDENT KINASE 2 (E.C.2.7.11.22), CYCLIN-A2 Functional site 1) chain B residue 199 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 2) chain B residue 202 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 3) chain B residue 203 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 4) chain B residue 243 type sequence L description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 5) chain B residue 245 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 6) chain B residue 246 type sequence M description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 7) chain B residue 247 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC1 8) chain B residue 189 type sequence M description BINDING SITE FOR RESIDUE SGM B 1434 source : AC2 9) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE SGM B 1434 source : AC2 10) chain B residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM B 1434 source : AC2 11) chain B residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM B 1434 source : AC2 12) chain B residue 305 type sequence D description BINDING SITE FOR RESIDUE SGM B 1434 source : AC2 13) chain B residue 327 type sequence C description BINDING SITE FOR RESIDUE SGM B 1435 source : AC3 14) chain B residue 330 type sequence E description BINDING SITE FOR RESIDUE SGM B 1435 source : AC3 15) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 16) chain C residue 64 type sequence V description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 17) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 18) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 19) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 20) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 21) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 22) chain C residue 89 type sequence K description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 23) chain C residue 131 type sequence Q description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 24) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 25) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 26) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE T3C C 1297 source : AC4 27) chain D residue 202 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1433 source : AC5 28) chain D residue 203 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 1433 source : AC5 29) chain D residue 244 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1433 source : AC5 30) chain D residue 245 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1433 source : AC5 31) chain D residue 246 type sequence M description BINDING SITE FOR RESIDUE SO4 D 1433 source : AC5 32) chain D residue 247 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1433 source : AC5 33) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE SGM D 1434 source : AC6 34) chain D residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM D 1434 source : AC6 35) chain D residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM D 1434 source : AC6 36) chain D residue 305 type sequence D description BINDING SITE FOR RESIDUE SGM D 1434 source : AC6 37) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 38) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 39) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 40) chain A residue 64 type sequence V description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 41) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 42) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 43) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 44) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 45) chain A residue 84 type sequence H description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 46) chain A residue 85 type sequence Q description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 47) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 48) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 49) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 50) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 51) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 52) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE T3C A 1299 source : AC7 53) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 54) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 55) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 56) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 57) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 58) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 60) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 61) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 62) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 63) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 64) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 65) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 66) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 67) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 68) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 82) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 83) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 84) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 85) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 86) 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 87) 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

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