eF-site ID 1gy3-ABCDEF PDB Code 1gy3 Chain A, B, C, D, E, F click to enlarge Title pCDK2/cyclin A in complex with MgADP, nitrate and peptide substrate Classification TRANSFERASE/TRANSFERASE SUBSTRATE Compound CELL DIVISION PROTEIN KINASE 2 Source (1GY3) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL B:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL D:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL E:  HHASPRK F:  HHASPRK Description Functional site 1) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 2) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 3) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 4) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 5) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 6) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 7) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 8) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 9) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 10) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 11) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 12) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP A 1297 source : AC1 13) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE MG A 1298 source : AC2 14) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE MG A 1298 source : AC2 15) chain A residue 127 type sequence D description BINDING SITE FOR RESIDUE NO3 A 1299 source : AC3 16) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE NO3 A 1299 source : AC3 17) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE NO3 A 1299 source : AC3 18) chain E residue 5 type sequence S description BINDING SITE FOR RESIDUE NO3 A 1299 source : AC3 19) chain B residue 211 type sequence R description BINDING SITE FOR RESIDUE GOL B 1433 source : AC4 20) chain B residue 240 type sequence D description BINDING SITE FOR RESIDUE GOL B 1433 source : AC4 21) chain B residue 340 type sequence S description BINDING SITE FOR RESIDUE GOL B 1433 source : AC4 22) chain B residue 341 type sequence L description BINDING SITE FOR RESIDUE GOL B 1433 source : AC4 23) chain B residue 348 type sequence L description BINDING SITE FOR RESIDUE GOL B 1433 source : AC4 24) chain B residue 246 type sequence M description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 25) chain C residue 23 type sequence N description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 26) chain C residue 28 type sequence E description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 27) chain C residue 68 type sequence D description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 28) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 29) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 30) chain C residue 33 type sequence K description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 31) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 32) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 33) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 34) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 35) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 36) chain C residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 37) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 38) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 39) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE MG C 1299 source : AC7 40) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE MG C 1299 source : AC7 41) chain C residue 127 type sequence D description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 42) chain C residue 129 type sequence K description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 43) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 44) chain F residue 5 type sequence S description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 45) chain A residue 127 type sequence D description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 46) chain A residue 129 type sequence K description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 47) chain A residue 160 type sequence X description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 48) chain A residue 162 type sequence E description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 49) chain A residue 164 type sequence V description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 50) chain A residue 165 type sequence T description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 51) chain B residue 270 type sequence I description BINDING SITE FOR CHAIN E OF SUBSTRATE PEPTIDE source : AC9 52) chain C residue 15 type sequence Y description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 53) chain C residue 50 type sequence R description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 54) chain C residue 127 type sequence D description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 55) chain C residue 129 type sequence K description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 56) chain C residue 148 type sequence L description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 57) chain C residue 160 type sequence X description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 58) chain C residue 162 type sequence E description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 59) chain C residue 163 type sequence V description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 60) chain C residue 164 type sequence V description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 61) chain C residue 165 type sequence T description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 62) chain C residue 166 type sequence L description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 63) chain C residue 167 type sequence W description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 64) chain C residue 169 type sequence R description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 65) chain C residue 205 type sequence G description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 66) chain D residue 269 type sequence E description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 67) chain D residue 270 type sequence I description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 68) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 69) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 84) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 85) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 86) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 87) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 88) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 89) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 90) 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 91) 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 92) 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 93) 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 94) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 95) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 96) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 97) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 98) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 99) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 100) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 101) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 102) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 103) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 104) 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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