eF-site ID 4bcn-ABCD PDB Code 4bcn 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 EGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFE FLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSH RVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYXH EVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRA LFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFP KWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAAL AHPFFQDVTKPVPHLRL B:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF LGELSLIDADPYLKYLPSVIAAAAFHLALYTVTGQSWPES LIRKTGYTLESLKPCLLDLHQTYLRAPKHAQQSIREKYKN SKYHGVSLLNPPETLNL C:  GSMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLD TETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYL VFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFC HSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRT YXHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVT RRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKP SFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAK AALAHPFFQDVTKPVP D:  DYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVD WLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLV GTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEH LVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFL GELSLIDADPYLKYLPSVIAAAAFHLALYTVTGQSWPESL IRKTGYTLESLKPCLLDLHQTYLKAPQHAQQSIREKYKNS KYHGVSLLNPPETLN Description (1)  CYCLIN-DEPENDENT KINASE 2 (E.C.2.7.11.22), CYCLIN-A2 Functional site 1) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 2) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 3) chain A residue 64 type sequence V description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 4) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 5) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 6) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 7) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 8) chain A residue 84 type sequence H description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 9) chain A residue 85 type sequence Q description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 10) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 11) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 12) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 13) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 14) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE T9N A 1299 source : AC1 15) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 16) chain C residue 64 type sequence V description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 17) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 18) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 19) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 20) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 21) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 22) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 23) chain C residue 89 type sequence K description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 24) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 25) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 26) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE T9N C 1296 source : AC2 27) chain B residue 199 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 28) chain B residue 202 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 29) chain B residue 203 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 30) chain B residue 243 type sequence L description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 31) chain B residue 245 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 32) chain B residue 246 type sequence M description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 33) chain B residue 247 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1433 source : AC3 34) chain D residue 199 type sequence Y description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 35) chain D residue 202 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 36) chain D residue 203 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 37) chain D residue 243 type sequence L description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 38) chain D residue 244 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 39) chain D residue 245 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 40) chain D residue 246 type sequence M description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 41) chain D residue 247 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1432 source : AC4 42) 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 43) 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 44) 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 45) 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 46) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 47) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 48) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 49) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 51) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 52) 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 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 66) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 67) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 68) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 69) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 70) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 71) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 72) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 73) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 74) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 75) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 76) chain D residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 77) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 78) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 79) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108

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