eF-site ID 2cch-A PDB Code 2cch Chain A 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 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 A residue 109 type sequence F description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 24) chain A residue 209 type sequence I description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 25) chain A residue 213 type sequence F description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 26) chain A residue 237 type sequence K description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 27) chain A residue 239 type sequence S description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 28) chain A residue 286 type sequence F description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 29) chain A residue 287 type sequence Q description BINDING SITE FOR RESIDUE GOL A1299 source : AC4 30) chain A residue 60 type sequence H description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 31) chain A residue 113 type sequence Q description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 32) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 33) chain A residue 117 type sequence F description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 34) chain A residue 242 type sequence K description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 35) chain A residue 243 type sequence W description BINDING SITE FOR RESIDUE GOL A1300 source : AC5 36) 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 37) 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 38) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 39) 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 40) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 43) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 44) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 45) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 47) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 48) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 49) 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 50) 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 51) 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 52) 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 53) 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 54) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links