eF-site ID 2uue-ABCDEF PDB Code 2uue Chain A, B, C, D, E, F click to enlarge Title REPLACE: A strategy for Iterative Design of Cyclin Binding Groove Inhibitors Classification TRANSFERASE/INHIBITOR Compound CELL DIVISION PROTEIN KINASE 2 Source (2UUE) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL B:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHLR D:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL E:  RLIXX F:  RLIXX Description Functional site 1) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 2) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 3) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 4) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 5) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 6) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 7) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 8) chain A residue 84 type sequence H description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 9) chain A residue 85 type sequence Q description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 10) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 11) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 12) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE MTZ A 1297 source : AC1 13) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 14) chain C residue 12 type sequence E description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 15) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 16) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 17) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 18) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 19) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 20) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE MTZ C 1298 source : AC2 21) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 22) chain B residue 217 type sequence W description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 23) chain B residue 220 type sequence E description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 24) chain B residue 221 type sequence V description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 25) chain B residue 254 type sequence Q description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 26) chain B residue 281 type sequence I description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 27) chain B residue 283 type sequence D description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 28) chain E residue 1 type sequence R description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 29) chain E residue 2 type sequence L description BINDING SITE FOR RESIDUE GVC E 1433 source : AC3 30) chain D residue 217 type sequence W description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 31) chain D residue 220 type sequence E description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 32) chain D residue 221 type sequence V description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 33) chain D residue 254 type sequence Q description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 34) chain D residue 281 type sequence I description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 35) chain D residue 282 type sequence T description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 36) chain D residue 283 type sequence D description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 37) chain F residue 1 type sequence R description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 38) chain F residue 2 type sequence L description BINDING SITE FOR RESIDUE GVC F 1433 source : AC4 39) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 40) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 41) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 42) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 43) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 44) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 45) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 46) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 47) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 49) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 50) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 52) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 53) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 54) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 55) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 56) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 57) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 75) 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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