eF-site ID 1oiu-C PDB Code 1oiu Chain C 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 C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGVPPLDEDGRSLLSQMLHYD PNKRISAKAALAHPFFQDVTKPVPHL Description Functional site 1) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 2) chain C residue 12 type sequence E description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 3) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 4) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 5) chain C residue 64 type sequence V description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 6) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 7) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 8) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 9) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 10) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 11) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 12) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 13) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE N76 C1298 source : AC3 14) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 15) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 18) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 19) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 20) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 21) 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 22) 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 23) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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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