eF-site ID 1h26-C PDB Code 1h26 Chain C click to enlarge Title CDK2/CyclinA in complex with an 11-residue recruitment peptide from p53 Classification CELL CYCLE Compound CELL DIVISION PROTEIN KINASE 2 Source null (P53_HUMAN) Sequence C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR RALFPGDSEIDQLFRIFRTLGTVVPPLDEDGRSLLSQMLH YDPNKRISAKAALAHPFFQDVTKPVPHLR Description Functional site 1) chain C residue 129 type MOD_RES sequence K description N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287 source Swiss-Prot : SWS_FT_FI2 2) chain C residue 10 type MOD_RES sequence I description N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287 source Swiss-Prot : SWS_FT_FI2 3) chain C residue 33 type MOD_RES sequence K description N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287 source Swiss-Prot : SWS_FT_FI2 4) chain C residue 81 type MOD_RES sequence E description N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287 source Swiss-Prot : SWS_FT_FI2 5) chain C residue 86 type MOD_RES sequence D description N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287 source Swiss-Prot : SWS_FT_FI2 6) chain C residue 132 type CROSSLNK sequence N description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37 source Swiss-Prot : SWS_FT_FI3 7) chain C residue 145 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37 source Swiss-Prot : SWS_FT_FI3 8) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 9) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 10) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 11) chain C residue 127 type MOD_RES sequence D description N6-acetyllysine => ECO:0000269|PubMed:29474172, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 12) 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 13) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 14) 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 15) 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 16) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 17) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links