eF-site ID 1h01-A PDB Code 1h01 Chain A click to enlarge Title CDK2 in complex with a disubstituted 2, 4-bis anilino pyrimidine CDK4 inhibitor Classification TRANSFERASE Compound CYCLIN-DEPENDENT KINASE 2 Source Homo sapiens (Human) (CDK2_HUMAN) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALXKIRSTAI REISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKK FMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLK PQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYR APEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEI DQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFS KVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDV TKPVPHL Description (1)  CYCLIN-DEPENDENT KINASE 2 (E.C.2.7.11.22) Functional site 1) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE GOL A 299 source : AC1 2) chain A residue 167 type sequence W description BINDING SITE FOR RESIDUE GOL A 299 source : AC1 3) chain A residue 168 type sequence Y description BINDING SITE FOR RESIDUE GOL A 299 source : AC1 4) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE GOL A 300 source : AC2 5) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE GOL A 300 source : AC2 6) chain A residue 14 type sequence T description BINDING SITE FOR RESIDUE GOL A 300 source : AC2 7) chain A residue 129 type sequence K description BINDING SITE FOR RESIDUE GOL A 300 source : AC2 8) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE GOL A 300 source : AC2 9) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 10) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 11) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 12) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 13) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 14) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 15) chain A residue 84 type sequence H description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 16) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 17) chain A residue 144 type sequence A description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 18) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE FAL A 301 source : AC3 19) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 20) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 21) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 22) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 23) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 24) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 25) chain A residue 84 type sequence H description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 26) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 27) chain A residue 88 type sequence K description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 28) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 29) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 30) chain A residue 144 type sequence A description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 31) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE FBL A 302 source : AC4 32) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALX description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 33) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 34) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 35) chain A 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 36) 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 37) chain A residue 33 type BINDING sequence X description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 38) 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 39) 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 40) 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 41) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 9 type SITE sequence K description CDK7 binding => ECO:0000269|PubMed:17373709 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 88 type SITE sequence K description CDK7 binding => ECO:0000269|PubMed:17373709 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 166 type SITE sequence L description CDK7 binding => ECO:0000269|PubMed:17373709 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 48) 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 49) 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 50) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9

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