eF-site ID 4eok-ABCD PDB Code 4eok Chain A, B, C, D click to enlarge Title Thr 160 phosphorylated CDK2 H84S, Q85M, K89D - human cyclin A3 complex with the inhibitor NU6102 Classification Transferase/Transferase Inhibitor Compound Cyclin-dependent kinase 2 Source Homo sapiens (Human) (CCNA2_HUMAN) Sequence A:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLEG VPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL SMDLKDFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRV LHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYXHEV VTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALF PGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKW ARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAH PFFQDVTKPVPHLR B:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL C:  LGSMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRL DTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLY LVFEFLSMDLKDFMDASALTGIPLPLIKSYLFQLLQGLAF CHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR TYXHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMV TRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYK PSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISA KAALAHPFFQDVTKPVPHLR D:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF LGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPES LIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN SKYHGVSLLNPPETLN Description (1)  Cyclin-dependent kinase 2 (E.C.2.7.11.22), Cyclin-A2 Functional site 1) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 2) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 3) chain A residue 64 type sequence V description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 4) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 5) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 6) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 7) chain A residue 84 type sequence S description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 8) chain A residue 85 type sequence M description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 9) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 10) chain A residue 89 type sequence D description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 11) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 12) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 13) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE 4SP A 301 source : AC1 14) chain B residue 189 type sequence M description BINDING SITE FOR RESIDUE SGM B 501 source : AC2 15) chain B residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM B 501 source : AC2 16) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 17) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 18) chain C residue 64 type sequence V description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 19) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 20) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 21) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 22) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 23) chain C residue 84 type sequence S description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 24) chain C residue 85 type sequence M description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 25) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 26) chain C residue 89 type sequence D description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 27) chain C residue 131 type sequence Q description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 28) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 29) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 30) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE 4SP C 301 source : AC3 31) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE SGM D 501 source : AC4 32) chain D residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM D 501 source : AC4 33) chain D residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM D 501 source : AC4 34) chain D residue 305 type sequence D description BINDING SITE FOR RESIDUE SGM D 501 source : AC4 35) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 36) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 37) 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 38) 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 39) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 40) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 41) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 42) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 44) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 45) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 46) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 47) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 48) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 49) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 50) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 51) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 52) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 53) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 54) 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 55) 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 56) 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 57) 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 58) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 59) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 71) 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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