eF-site ID 4zse-C PDB Code 4zse Chain C click to enlarge Title Crystal structure of EGFR 696-1022 T790M/V948R, crystal form II Classification TRANSFERASE Compound Epidermal growth factor receptor Source Homo sapiens (Human) (EGFR_HUMAN) Sequence C:  NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVK IPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLG ICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCV QIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA KLLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGS KPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWM IDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSP TDSNFYRALMDEEDMDDVVDA Description Functional site 1) chain C residue 718 type sequence L description binding site for residue ANP C 3001 source : AC5 2) chain C residue 719 type sequence G description binding site for residue ANP C 3001 source : AC5 3) chain C residue 720 type sequence S description binding site for residue ANP C 3001 source : AC5 4) chain C residue 721 type sequence G description binding site for residue ANP C 3001 source : AC5 5) chain C residue 722 type sequence A description binding site for residue ANP C 3001 source : AC5 6) chain C residue 724 type sequence G description binding site for residue ANP C 3001 source : AC5 7) chain C residue 726 type sequence V description binding site for residue ANP C 3001 source : AC5 8) chain C residue 743 type sequence A description binding site for residue ANP C 3001 source : AC5 9) chain C residue 745 type sequence K description binding site for residue ANP C 3001 source : AC5 10) chain C residue 790 type sequence M description binding site for residue ANP C 3001 source : AC5 11) chain C residue 791 type sequence Q description binding site for residue ANP C 3001 source : AC5 12) chain C residue 793 type sequence M description binding site for residue ANP C 3001 source : AC5 13) chain C residue 797 type sequence C description binding site for residue ANP C 3001 source : AC5 14) chain C residue 837 type sequence D description binding site for residue ANP C 3001 source : AC5 15) chain C residue 841 type sequence R description binding site for residue ANP C 3001 source : AC5 16) chain C residue 842 type sequence N description binding site for residue ANP C 3001 source : AC5 17) chain C residue 844 type sequence L description binding site for residue ANP C 3001 source : AC5 18) chain C residue 855 type sequence D description binding site for residue ANP C 3001 source : AC5 19) chain C residue 842 type sequence N description binding site for residue MG C 3002 source : AC6 20) chain C residue 855 type sequence D description binding site for residue MG C 3002 source : AC6 21) chain C residue 808 type sequence N description binding site for residue EDO C 3003 source : AC7 22) chain C residue 813 type sequence Y description binding site for residue EDO C 3003 source : AC7 23) chain C 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 24) chain C 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 25) chain C 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 26) chain C 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_FI15 27) chain C 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_FI15 28) chain C 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_FI16 29) chain C 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_FI16 30) chain C 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_FI14 31) chain C 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_FI14 32) chain C 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_FI14 33) chain C 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_FI10 34) chain C residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 35) chain C residue 998 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI12 36) chain C residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI8 37) chain C 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 38) chain C 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

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