eF-site ID 1gy3-C PDB Code 1gy3 Chain C 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 C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL Description Functional site 1) chain C residue 23 type sequence N description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 2) chain C residue 28 type sequence E description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 3) chain C residue 68 type sequence D description BINDING SITE FOR RESIDUE GOL C 1297 source : AC5 4) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 5) chain C residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 6) chain C residue 33 type sequence K description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 7) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 8) chain C residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 9) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 10) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 11) chain C residue 86 type sequence D description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 12) chain C residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 13) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 14) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP C 1298 source : AC6 15) chain C residue 132 type sequence N description BINDING SITE FOR RESIDUE MG C 1299 source : AC7 16) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE MG C 1299 source : AC7 17) chain C residue 127 type sequence D description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 18) chain C residue 129 type sequence K description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 19) chain C residue 145 type sequence D description BINDING SITE FOR RESIDUE NO3 C 1300 source : AC8 20) chain C residue 15 type sequence Y description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 21) chain C residue 50 type sequence R description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 22) chain C residue 127 type sequence D description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 23) chain C residue 129 type sequence K description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 24) chain C residue 148 type sequence L description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 25) chain C residue 160 type sequence X description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 26) chain C residue 162 type sequence E description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 27) chain C residue 163 type sequence V description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 28) chain C residue 164 type sequence V description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 29) chain C residue 165 type sequence T description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 30) chain C residue 166 type sequence L description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 31) chain C residue 167 type sequence W description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 32) chain C residue 169 type sequence R description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 33) chain C residue 205 type sequence G description BINDING SITE FOR CHAIN F OF SUBSTRATE PEPTIDE source : BC1 34) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 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 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 39) 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 40) 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 41) 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 42) 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 43) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 44) 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 45) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 46) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 47) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 48) 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 49) 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 50) 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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