eF-site ID 2cch-ABCDEF PDB Code 2cch Chain A, B, C, D, E, F click to enlarge Title The crystal structure of CDK2 cyclin A in complex with a substrate peptide derived from CDC modified with a gamma-linked ATP analogue Classification CELL CYCLE Compound CELL DIVISION PROTEIN KINASE 2 Source (CDC6_HUMAN) Sequence A:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKA ALAHPFFQDVTKPVPHL B:  NEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRA ILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGK LQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESL AMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSW PESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK YKNSKYHGVSLLNPPETLNL C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKA ALAHPFFQDVTKPVPHL D:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF LGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPES LIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN SKYHGVSLLNPPETLN E:  HTLKGRRLVFDN F:  HTLKGRRLVFDN Description Functional site 1) chain A residue 214 type sequence R description BINDING SITE FOR RESIDUE SO4 A1298 source : AC1 2) chain A residue 217 type sequence R description BINDING SITE FOR RESIDUE SO4 A1298 source : AC1 3) chain A residue 278 type sequence K description BINDING SITE FOR RESIDUE SO4 A1298 source : AC1 4) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 5) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 6) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 7) chain A residue 15 type sequence Y description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 8) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 9) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 10) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 11) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 12) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 13) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 14) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 15) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 16) chain A residue 129 type sequence K description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 17) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 18) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 19) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 20) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 21) chain A residue 147 type sequence G description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 22) chain A residue 148 type sequence L description BINDING SITE FOR RESIDUE ATP A1297 source : AC2 23) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 24) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 25) chain C residue 12 type sequence E description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 26) chain C residue 15 type sequence Y description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 27) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 28) chain C residue 33 type sequence K description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 29) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 30) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 31) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 32) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 33) chain C residue 89 type sequence K description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 34) chain C residue 129 type sequence K description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 35) chain C residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 36) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 37) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 38) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 39) chain C residue 147 type sequence G description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 40) chain C residue 148 type sequence L description BINDING SITE FOR RESIDUE ATP C1297 source : AC3 41) chain A residue 109 type sequence F description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 42) chain A residue 209 type sequence I description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 43) chain A residue 213 type sequence F description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 44) chain A residue 237 type sequence K description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 45) chain A residue 239 type sequence S description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 46) chain A residue 286 type sequence F description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 47) chain A residue 287 type sequence Q description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 48) chain A residue 60 type sequence H description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 49) chain A residue 113 type sequence Q description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 50) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 51) chain A residue 117 type sequence F description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 52) chain A residue 242 type sequence K description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 53) chain A residue 243 type sequence W description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 54) 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 55) 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 56) 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 57) 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 58) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 59) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 60) 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 61) 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 62) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 63) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 64) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 65) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 66) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 67) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 68) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 69) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 70) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 71) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 72) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 73) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 74) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 75) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 76) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 77) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 78) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 79) 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 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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 86) 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 87) 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 88) 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 89) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 90) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

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