eF-site ID 1fin-ABCD PDB Code 1fin Chain A, B, C, D click to enlarge Title CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX Classification COMPLEX (TRANSFERASE/CYCLIN) Compound CYCLIN-DEPENDENT KINASE 2 Source null (CCNA2_HUMAN) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHLRL B:  NEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRA ILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGK LQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESL AMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSW PESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK YKNSKYHGVSLLNPPETLNL C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHLRL D:  NEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRA ILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGK LQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESL AMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSW PESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK YKNSKYHGVSLLNPPETLNL Description Functional site 1) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 2) chain A residue 12 type sequence E description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 3) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 4) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 5) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 6) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 7) chain A residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 8) chain A residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 9) chain A residue 134 type sequence L description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 10) chain A residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP A 299 source : AC1 11) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 12) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 13) chain C residue 12 type sequence E description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 14) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 15) chain C residue 14 type sequence T description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 16) chain C residue 18 type sequence V description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 17) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 18) chain C residue 64 type sequence V description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 19) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 20) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 21) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP C 299 source : AC2 22) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 23) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 24) 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 25) 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 26) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 27) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 28) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 29) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 34) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 35) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 36) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 37) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 38) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 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 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 44) 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 45) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 46) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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 57) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 58) 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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