eF-site ID 4zse-ABCD PDB Code 4zse Chain A, B, C, D 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 A:  PNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKV KIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLL GICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWC VQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGL AKLLKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTF GSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKC WMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLP SPTDSNFYRALMDEEDM B:  APNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEK VKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRL LGICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNW CVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFG LAKLLKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMT FGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRK CWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHL PSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG C:  NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVK IPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLG ICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCV QIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA KLLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGS KPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWM IDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSP TDSNFYRALMDEEDMDDVVDA D:  QALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKI PVAIKELRESPKANKEILDEAYVMASVDNPHVCRLLGICL TSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIA KGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLL GVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKP YDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWMID ADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTD SNFYRALMDEEVVDADE Description Functional site 1) chain A residue 718 type sequence L description binding site for residue ANP A 1101 source : AC1 2) chain A residue 719 type sequence G description binding site for residue ANP A 1101 source : AC1 3) chain A residue 720 type sequence S description binding site for residue ANP A 1101 source : AC1 4) chain A residue 721 type sequence G description binding site for residue ANP A 1101 source : AC1 5) chain A residue 722 type sequence A description binding site for residue ANP A 1101 source : AC1 6) chain A residue 724 type sequence G description binding site for residue ANP A 1101 source : AC1 7) chain A residue 726 type sequence V description binding site for residue ANP A 1101 source : AC1 8) chain A residue 743 type sequence A description binding site for residue ANP A 1101 source : AC1 9) chain A residue 745 type sequence K description binding site for residue ANP A 1101 source : AC1 10) chain A residue 790 type sequence M description binding site for residue ANP A 1101 source : AC1 11) chain A residue 791 type sequence Q description binding site for residue ANP A 1101 source : AC1 12) chain A residue 793 type sequence M description binding site for residue ANP A 1101 source : AC1 13) chain A residue 797 type sequence C description binding site for residue ANP A 1101 source : AC1 14) chain A residue 837 type sequence D description binding site for residue ANP A 1101 source : AC1 15) chain A residue 841 type sequence R description binding site for residue ANP A 1101 source : AC1 16) chain A residue 842 type sequence N description binding site for residue ANP A 1101 source : AC1 17) chain A residue 844 type sequence L description binding site for residue ANP A 1101 source : AC1 18) chain A residue 855 type sequence D description binding site for residue ANP A 1101 source : AC1 19) chain A residue 842 type sequence N description binding site for residue MG A 1102 source : AC2 20) chain A residue 855 type sequence D description binding site for residue MG A 1102 source : AC2 21) chain B residue 718 type sequence L description binding site for residue ANP B 2001 source : AC3 22) chain B residue 719 type sequence G description binding site for residue ANP B 2001 source : AC3 23) chain B residue 721 type sequence G description binding site for residue ANP B 2001 source : AC3 24) chain B residue 722 type sequence A description binding site for residue ANP B 2001 source : AC3 25) chain B residue 724 type sequence G description binding site for residue ANP B 2001 source : AC3 26) chain B residue 726 type sequence V description binding site for residue ANP B 2001 source : AC3 27) chain B residue 743 type sequence A description binding site for residue ANP B 2001 source : AC3 28) chain B residue 745 type sequence K description binding site for residue ANP B 2001 source : AC3 29) chain B residue 790 type sequence M description binding site for residue ANP B 2001 source : AC3 30) chain B residue 791 type sequence Q description binding site for residue ANP B 2001 source : AC3 31) chain B residue 793 type sequence M description binding site for residue ANP B 2001 source : AC3 32) chain B residue 797 type sequence C description binding site for residue ANP B 2001 source : AC3 33) chain B residue 837 type sequence D description binding site for residue ANP B 2001 source : AC3 34) chain B residue 841 type sequence R description binding site for residue ANP B 2001 source : AC3 35) chain B residue 842 type sequence N description binding site for residue ANP B 2001 source : AC3 36) chain B residue 844 type sequence L description binding site for residue ANP B 2001 source : AC3 37) chain B residue 855 type sequence D description binding site for residue ANP B 2001 source : AC3 38) chain B residue 842 type sequence N description binding site for residue MG B 2002 source : AC4 39) chain B residue 855 type sequence D description binding site for residue MG B 2002 source : AC4 40) chain C residue 718 type sequence L description binding site for residue ANP C 3001 source : AC5 41) chain C residue 719 type sequence G description binding site for residue ANP C 3001 source : AC5 42) chain C residue 720 type sequence S description binding site for residue ANP C 3001 source : AC5 43) chain C residue 721 type sequence G description binding site for residue ANP C 3001 source : AC5 44) chain C residue 722 type sequence A description binding site for residue ANP C 3001 source : AC5 45) chain C residue 724 type sequence G description binding site for residue ANP C 3001 source : AC5 46) chain C residue 726 type sequence V description binding site for residue ANP C 3001 source : AC5 47) chain C residue 743 type sequence A description binding site for residue ANP C 3001 source : AC5 48) chain C residue 745 type sequence K description binding site for residue ANP C 3001 source : AC5 49) chain C residue 790 type sequence M description binding site for residue ANP C 3001 source : AC5 50) chain C residue 791 type sequence Q description binding site for residue ANP C 3001 source : AC5 51) chain C residue 793 type sequence M description binding site for residue ANP C 3001 source : AC5 52) chain C residue 797 type sequence C description binding site for residue ANP C 3001 source : AC5 53) chain C residue 837 type sequence D description binding site for residue ANP C 3001 source : AC5 54) chain C residue 841 type sequence R description binding site for residue ANP C 3001 source : AC5 55) chain C residue 842 type sequence N description binding site for residue ANP C 3001 source : AC5 56) chain C residue 844 type sequence L description binding site for residue ANP C 3001 source : AC5 57) chain C residue 855 type sequence D description binding site for residue ANP C 3001 source : AC5 58) chain C residue 842 type sequence N description binding site for residue MG C 3002 source : AC6 59) chain C residue 855 type sequence D description binding site for residue MG C 3002 source : AC6 60) chain C residue 808 type sequence N description binding site for residue EDO C 3003 source : AC7 61) chain C residue 813 type sequence Y description binding site for residue EDO C 3003 source : AC7 62) chain D residue 719 type sequence G description binding site for residue ANP D 4001 source : AC8 63) chain D residue 720 type sequence S description binding site for residue ANP D 4001 source : AC8 64) chain D residue 721 type sequence G description binding site for residue ANP D 4001 source : AC8 65) chain D residue 722 type sequence A description binding site for residue ANP D 4001 source : AC8 66) chain D residue 724 type sequence G description binding site for residue ANP D 4001 source : AC8 67) chain D residue 726 type sequence V description binding site for residue ANP D 4001 source : AC8 68) chain D residue 743 type sequence A description binding site for residue ANP D 4001 source : AC8 69) chain D residue 745 type sequence K description binding site for residue ANP D 4001 source : AC8 70) chain D residue 790 type sequence M description binding site for residue ANP D 4001 source : AC8 71) chain D residue 791 type sequence Q description binding site for residue ANP D 4001 source : AC8 72) chain D residue 793 type sequence M description binding site for residue ANP D 4001 source : AC8 73) chain D residue 797 type sequence C description binding site for residue ANP D 4001 source : AC8 74) chain D residue 837 type sequence D description binding site for residue ANP D 4001 source : AC8 75) chain D residue 841 type sequence R description binding site for residue ANP D 4001 source : AC8 76) chain D residue 842 type sequence N description binding site for residue ANP D 4001 source : AC8 77) chain D residue 844 type sequence L description binding site for residue ANP D 4001 source : AC8 78) chain D residue 855 type sequence D description binding site for residue ANP D 4001 source : AC8 79) chain D residue 842 type sequence N description binding site for residue MG D 4002 source : AC9 80) chain D residue 855 type sequence D description binding site for residue MG D 4002 source : AC9 81) 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 82) chain B 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 83) 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 84) chain D 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 85) chain B residue 1016 type SITE sequence Y description Important for interaction with PIK3C2B source Swiss-Prot : SWS_FT_FI6 86) 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 87) chain B 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 88) 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 89) chain D 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 90) 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 91) chain B 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 92) 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 93) chain D 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 94) 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_FI10 95) chain B 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 96) 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 97) chain D 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 98) 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 99) chain B 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 100) 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 101) chain D 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 102) 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 103) chain B 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 104) 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 105) chain D 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 106) chain B residue 1016 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:23774213 source Swiss-Prot : SWS_FT_FI13 107) chain A residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 108) chain B residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 109) chain C residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 110) chain D residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 111) 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_FI12 112) chain B 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 113) 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 114) chain D 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 115) chain A residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI8 116) chain B residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI8 117) chain C residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI8 118) chain D residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI8 119) chain D 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 120) chain D 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 121) 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_FI15 122) 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_FI15 123) chain B 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 124) chain B 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 125) 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 126) 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 127) 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_FI16 128) 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_FI16 129) chain B 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 130) chain B 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 131) 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 132) 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 133) chain D 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 134) chain D 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 135) 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_FI14 136) 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 137) 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 138) chain D 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 139) chain D 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 140) chain D 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 141) 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_FI14 142) 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_FI14 143) chain B 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 144) chain B 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 145) chain B 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 146) 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 147) chain A residue 718-745 type prosite sequence LGSGAFGTVYKGLWIPEGEKVKIPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK source prosite : PS00107 148) chain A residue 833-845 type prosite sequence LVHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV source prosite : PS00109

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