eF-site ID 1dm2-A PDB Code 1dm2 Chain A click to enlarge Title HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR HYMENIALDISINE Classification CELL CYCLE Compound CYCLIN-DEPENDENT KINASE 2 Source null (CDK2_HUMAN) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIPSTAI REISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKK FMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLK PQNLLINTEGAIKLADFGLVTLWYRAPEILLGCKYYSTAV DIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDE VVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLS QMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL Description Functional site 1) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 2) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 3) chain A residue 64 type sequence V description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 4) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 5) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 6) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 7) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 8) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 9) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 10) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE HMD A 400 source : AC1 11) chain A residue 88 type sequence K description BINDING SITE FOR RESIDUE EDO A 401 source : AC2 12) chain A residue 130 type sequence P description BINDING SITE FOR RESIDUE EDO A 401 source : AC2 13) chain A residue 167 type sequence W description BINDING SITE FOR RESIDUE EDO A 401 source : AC2 14) chain A residue 168 type sequence Y description BINDING SITE FOR RESIDUE EDO A 401 source : AC2 15) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE EDO A 401 source : AC2 16) chain A residue 91 type sequence M description BINDING SITE FOR RESIDUE EDO A 402 source : AC3 17) chain A residue 92 type sequence D description BINDING SITE FOR RESIDUE EDO A 402 source : AC3 18) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE EDO A 402 source : AC3 19) chain A residue 199 type sequence R description BINDING SITE FOR RESIDUE EDO A 402 source : AC3 20) chain A residue 136 type sequence N description BINDING SITE FOR RESIDUE EDO A 403 source : AC4 21) chain A residue 137 type sequence T description BINDING SITE FOR RESIDUE EDO A 403 source : AC4 22) chain A residue 257 type sequence E description BINDING SITE FOR RESIDUE EDO A 403 source : AC4 23) chain A residue 261 type sequence S description BINDING SITE FOR RESIDUE EDO A 403 source : AC4 24) chain A residue 137 type sequence T description BINDING SITE FOR RESIDUE EDO A 404 source : AC5 25) chain A residue 265 type sequence Q description BINDING SITE FOR RESIDUE EDO A 404 source : AC5 26) chain A residue 268 type sequence H description BINDING SITE FOR RESIDUE EDO A 404 source : AC5 27) chain A residue 294 type sequence P description BINDING SITE FOR RESIDUE EDO A 404 source : AC5 28) chain A residue 295 type sequence H description BINDING SITE FOR RESIDUE EDO A 404 source : AC5 29) chain A residue 296 type sequence L description BINDING SITE FOR RESIDUE EDO A 404 source : AC5 30) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 31) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 32) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 35) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 36) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 37) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 38) 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 39) 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 40) 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 41) 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 42) 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 43) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 45) 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 46) 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 47) 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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