eF-site ID 2uzl-C PDB Code 2uzl Chain C click to enlarge Title Crystal structure of human CDK2 complexed with a thiazolidinone inhibitor Classification TRANSFERASE Compound CELL DIVISION PROTEIN KINASE 2 Source (CCNA2_HUMAN) Sequence C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHLR Description (1)  CELL DIVISION PROTEIN KINASE 2 (E.C.2.7.11.22, 2.7.1.37), CYCLIN A2 Functional site 1) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 2) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 3) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 4) chain C residue 33 type sequence K description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 5) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 6) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 7) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 8) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 9) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 10) chain C residue 85 type sequence Q description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 11) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 12) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 13) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE C94 C1297 source : AC2 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 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 22) 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 23) 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 24) 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 25) 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 26) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 27) 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 28) 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 29) 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 30) 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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