eF-site ID 1vyw-C PDB Code 1vyw Chain C click to enlarge Title Structure of CDK2/Cyclin A with PNU-292137 Classification TRANSFERASE Compound CELL DIVISION PROTEIN KINASE 2 Source (CGA2_HUMAN) Sequence C:  DMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY THEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKA ALAHPFFQDVTKPVPHLRL Description Functional site 1) chain C residue 8 type sequence E description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 2) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 3) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 4) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 5) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 6) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 7) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 8) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 9) chain C residue 89 type sequence K description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 10) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE 292 C 2300 source : AC4 11) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 12) chain C 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 13) 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 14) 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 15) 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 16) 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 17) 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 18) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 9 type SITE sequence K description CDK7 binding => ECO:0000269|PubMed:17373709 source Swiss-Prot : SWS_FT_FI4 21) chain C residue 88 type SITE sequence K description CDK7 binding => ECO:0000269|PubMed:17373709 source Swiss-Prot : SWS_FT_FI4 22) chain C residue 166 type SITE sequence L description CDK7 binding => ECO:0000269|PubMed:17373709 source Swiss-Prot : SWS_FT_FI4 23) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 24) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 25) 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 26) 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 27) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9

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