eF-site ID 3my5-ABCD PDB Code 3my5 Chain A, B, C, D click to enlarge Title CDk2/cyclinA in complex with DRB Classification TRANSFERASE/PROTEIN BINDING/INHIBITOR Compound Cell division protein kinase 2 Source Homo sapiens (Human) (CCNA2_BOVIN) Sequence A:  GSMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLT EGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFE FLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSH RVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYXH EVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRA LFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFP KWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAAL AHPFFQDVTKPVPHLRL B:  SVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSM RAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLR GKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQ VLRMEHLVLKVLAFDLAAPTINQFLTQYFLHQQPANCKVE SLAMFLGELSLIDADPYLKYLPSVIAAAAFHLALYTVTGQ SWPESLVQKTGYTLETLKPCLLDLHQTYLRAPQHAQQSIR EKYKNSKYHGVSLLNPPETLNV C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGVVPPLDEDGRSLLSQMLHY DPNKRISAKAALAHPFFQDVTKPVPHL D:  SVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSM RAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLR GKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQ VLRMEHLVLKVLAFDLAAPTINQFLTQYFLHQQPANCKVE SLAMFLGELSLIDADPYLKYLPSVIAAAAFHLALYTVTGQ SWPESLVQKTGYTLETLKPCLLDLHQTYLRAPQHAQQSIR EKYKNSKYHGVSLLNPPETLNV Description Functional site 1) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 2) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 3) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 4) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 5) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 6) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 7) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 8) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 9) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE RFZ A 300 source : AC1 10) chain A residue 226 type sequence V description BINDING SITE FOR RESIDUE FMT A 301 source : AC2 11) chain A residue 268 type sequence H description BINDING SITE FOR RESIDUE FMT A 301 source : AC2 12) chain A residue 269 type sequence Y description BINDING SITE FOR RESIDUE FMT A 301 source : AC2 13) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE SGM B 1 source : AC3 14) chain B residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM B 1 source : AC3 15) chain B residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM B 1 source : AC3 16) chain B residue 305 type sequence D description BINDING SITE FOR RESIDUE SGM B 1 source : AC3 17) chain A residue 182 type sequence T description BINDING SITE FOR RESIDUE FMT B 2 source : AC4 18) chain A residue 276 type sequence S description BINDING SITE FOR RESIDUE FMT B 2 source : AC4 19) chain B residue 175 type sequence V description BINDING SITE FOR RESIDUE FMT B 2 source : AC4 20) chain B residue 176 type sequence P description BINDING SITE FOR RESIDUE FMT B 2 source : AC4 21) chain B residue 177 type sequence D description BINDING SITE FOR RESIDUE FMT B 2 source : AC4 22) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 23) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 24) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 25) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 26) chain C residue 131 type sequence Q description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 27) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 28) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 29) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE RFZ C 301 source : AC5 30) chain D residue 193 type sequence C description BINDING SITE FOR RESIDUE SGM D 2 source : AC6 31) chain D residue 241 type sequence R description BINDING SITE FOR RESIDUE SGM D 2 source : AC6 32) chain D residue 305 type sequence D description BINDING SITE FOR RESIDUE SGM D 2 source : AC6 33) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 34) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 35) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 37) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 38) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 40) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 54) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 55) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 56) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 57) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 58) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 59) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 60) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 61) 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 62) 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 63) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 64) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 65) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 66) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 67) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 68) chain A 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 69) 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

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