eF-site ID 2vth-A PDB Code 2vth Chain A click to enlarge Title Identification of N-(4-piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), a Novel Cyclin Dependent Kinase Inhibitor Using Fragment-Based X-Ray Crystallography and Structure Based Drug Design Classification TRANSFERASE Compound CELL DIVISION PROTEIN KINASE 2 Source Homo sapiens (Human) (CDK2_HUMAN) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRSTAI REISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKK FMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLK PQNLLINTEGAIKLADFGLARAFVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLG TPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGR SLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL Description (1)  CELL DIVISION PROTEIN KINASE 2 (E.C.2.7.11.1, 2.7.11.22) Functional site 1) chain A residue 137 type sequence T description BINDING SITE FOR RESIDUE GOL A 1299 source : AC1 2) chain A residue 138 type sequence E description BINDING SITE FOR RESIDUE GOL A 1299 source : AC1 3) chain A residue 257 type sequence E description BINDING SITE FOR RESIDUE GOL A 1299 source : AC1 4) chain A residue 260 type sequence R description BINDING SITE FOR RESIDUE GOL A 1299 source : AC1 5) chain A residue 261 type sequence S description BINDING SITE FOR RESIDUE GOL A 1299 source : AC1 6) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 7) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 8) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 9) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 10) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 11) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 12) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 13) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE LZ2 A 1300 source : AC2 14) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 15) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 18) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 19) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 20) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 21) 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 22) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 23) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 24) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 25) 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 26) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 27) chain A 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 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 29) 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 30) 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 31) 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

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