eF-site ID 5zto-A PDB Code 5zto Chain A click to enlarge Title Crystal structure of EGFR 696-1022 T790M/C797S in complex with D3003 Classification TRANSFERASE Compound Epidermal growth factor receptor Source (EGFR_HUMAN) Sequence A:  EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGE KVKIPVAIKELATSPKANKEILDEAYVMASVDNPHVCRLL GICLTSTVQLIMQLMPFGSLLDYVREHKDNIGSQYLLNWC VQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGL APIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPY DGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDA DSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDS NFYMDDVVDADEYL Description Functional site 1) chain A residue 718 type sequence L description binding site for residue 9JO A 1101 source : AC1 2) chain A residue 719 type sequence G description binding site for residue 9JO A 1101 source : AC1 3) chain A residue 726 type sequence V description binding site for residue 9JO A 1101 source : AC1 4) chain A residue 743 type sequence A description binding site for residue 9JO A 1101 source : AC1 5) chain A residue 745 type sequence K description binding site for residue 9JO A 1101 source : AC1 6) chain A residue 762 type sequence E description binding site for residue 9JO A 1101 source : AC1 7) chain A residue 766 type sequence M description binding site for residue 9JO A 1101 source : AC1 8) chain A residue 790 type sequence M description binding site for residue 9JO A 1101 source : AC1 9) chain A residue 791 type sequence Q description binding site for residue 9JO A 1101 source : AC1 10) chain A residue 793 type sequence M description binding site for residue 9JO A 1101 source : AC1 11) chain A residue 794 type sequence P description binding site for residue 9JO A 1101 source : AC1 12) chain A residue 796 type sequence G description binding site for residue 9JO A 1101 source : AC1 13) chain A residue 877 type sequence P description binding site for residue CL A 1102 source : AC2 14) chain A residue 878 type sequence I description binding site for residue CL A 1102 source : AC2 15) chain A residue 879 type sequence K description binding site for residue CL A 1102 source : AC2 16) chain A residue 790 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 855 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 837 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 718 type BINDING sequence L description BINDING => ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 745 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 1016 type SITE sequence Y description Important for interaction with PIK3C2B source Swiss-Prot : SWS_FT_FI6 22) chain A residue 718-745 type prosite sequence LGSGAFGTVYKGLWIPEGEKVKIPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK source prosite : PS00107 23) chain A residue 833-845 type prosite sequence LVHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV source prosite : PS00109 24) chain A residue 929 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 25) chain A residue 970 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 26) chain A residue 757 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 27) chain A residue 960 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 28) chain A residue 716 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 29) chain A residue 754 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 30) chain A residue 737 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 31) chain A residue 1016 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:23774213 source Swiss-Prot : SWS_FT_FI12 32) chain A residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI10 33) chain A residue 998 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 34) chain A residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 35) chain A residue 991 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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