eF-site ID 2a0c-X PDB Code 2a0c Chain X click to enlarge Title Human CDK2 in complex with olomoucine II, a novel 2,6,9-trisubstituted purine cyclin-dependent kinase inhibitor Classification TRANSFERASE Compound Cell division protein kinase 2 Source Homo sapiens (Human) (CDK2_HUMAN) Sequence X:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRTEGV PSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLH QDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVL HRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVV TLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFP GDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWA RQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHP FFQDVTKPVPHLRL Description Functional site 1) chain X residue 10 type sequence I description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 2) chain X residue 11 type sequence G description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 3) chain X residue 12 type sequence E description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 4) chain X residue 18 type sequence V description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 5) chain X residue 31 type sequence A description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 6) chain X residue 80 type sequence F description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 7) chain X residue 81 type sequence E description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 8) chain X residue 83 type sequence L description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 9) chain X residue 84 type sequence H description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 10) chain X residue 89 type sequence K description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 11) chain X residue 131 type sequence Q description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 12) chain X residue 132 type sequence N description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 13) chain X residue 134 type sequence L description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 14) chain X residue 144 type sequence A description BINDING SITE FOR RESIDUE CK9 X 500 source : AC1 15) chain X residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 16) chain X residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 17) chain X residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 18) chain X residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 19) chain X residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 20) chain X residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 21) chain X residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 22) chain X residue 14 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 source Swiss-Prot : SWS_FT_FI7 23) chain X 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 24) chain X residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 25) chain X residue 160 type MOD_RES sequence T 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 26) chain X residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 27) chain X residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 28) chain X residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 29) chain X 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 30) chain X 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 31) chain X 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 32) chain X 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 33) chain X 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

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