eF-site ID 6q4d-A PDB Code 6q4d Chain A click to enlarge Title CDK2 in complex with FragLite31 Classification CELL CYCLE Compound Cyclin-dependent kinase 2 Source (CDK2_HUMAN) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLPST AIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDL KKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRD LKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLW YRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDS EIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQD FSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQ DVTKPVPHL Description Functional site 1) chain A residue 13 type sequence G description binding site for residue HHT A 301 source : AC1 2) chain A residue 14 type sequence T description binding site for residue HHT A 301 source : AC1 3) chain A residue 33 type sequence K description binding site for residue HHT A 301 source : AC1 4) chain A residue 129 type sequence K description binding site for residue HHT A 301 source : AC1 5) chain A residue 131 type sequence Q description binding site for residue HHT A 301 source : AC1 6) chain A residue 32 type sequence L description binding site for residue HHT A 302 source : AC2 7) chain A residue 34 type sequence K description binding site for residue HHT A 302 source : AC2 8) chain A residue 75 type sequence K description binding site for residue HHT A 302 source : AC2 9) chain A residue 77 type sequence Y description binding site for residue HHT A 302 source : AC2 10) chain A residue 1 type sequence M description binding site for residue HHT A 303 source : AC3 11) chain A residue 2 type sequence E description binding site for residue HHT A 303 source : AC3 12) chain A residue 3 type sequence N description binding site for residue HHT A 303 source : AC3 13) chain A residue 4 type sequence F description binding site for residue HHT A 303 source : AC3 14) chain A residue 73 type sequence E description binding site for residue HHT A 303 source : AC3 15) chain A residue 75 type sequence K description binding site for residue HHT A 303 source : AC3 16) chain A residue 77 type sequence Y description binding site for residue HHT A 303 source : AC3 17) chain A residue 122 type sequence R description binding site for residue HHT A 303 source : AC3 18) chain A residue 179 type sequence Y description binding site for residue HHT A 303 source : AC3 19) chain A residue 4 type sequence F description binding site for residue HHT A 304 source : AC4 20) chain A residue 6 type sequence K description binding site for residue HHT A 304 source : AC4 21) chain A residue 19 type sequence Y description binding site for residue HHT A 304 source : AC4 22) chain A residue 99 type sequence I description binding site for residue HHT A 305 source : AC5 23) chain A residue 100 type sequence P description binding site for residue HHT A 305 source : AC5 24) chain A residue 101 type sequence L description binding site for residue HHT A 305 source : AC5 25) chain A residue 109 type sequence F description binding site for residue HHT A 306 source : AC6 26) chain A residue 113 type sequence Q description binding site for residue HHT A 306 source : AC6 27) chain A residue 161 type sequence H description binding site for residue HHT A 306 source : AC6 28) chain A residue 281 type sequence L description binding site for residue HHT A 306 source : AC6 29) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 38) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 39) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 42) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 43) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 44) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 45) 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 46) 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 47) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9

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