eF-site ID 2itw-A PDB Code 2itw Chain A click to enlarge Title Crystal structure of EGFR kinase domain in complex with AFN941 Classification TRANSFERASE Compound EPIDERMAL GROWTH FACTOR RECEPTOR Source null (EGFR_HUMAN) Sequence A:  GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEG EKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVC RLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLL NWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITD FGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQS DVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQ PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDP QRYLVIQGDMDDVVDADEYLI Description Functional site 1) chain A residue 718 type sequence L description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 2) chain A residue 719 type sequence G description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 3) chain A residue 720 type sequence S description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 4) chain A residue 726 type sequence V description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 5) chain A residue 743 type sequence A description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 6) chain A residue 792 type sequence L description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 7) chain A residue 793 type sequence M description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 8) chain A residue 794 type sequence P description BINDING SITE FOR RESIDUE ITQ A 2018 source : AC1 9) 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 10) 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 11) 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 12) chain A residue 1016 type SITE sequence Y description Important for interaction with PIK3C2B source Swiss-Prot : SWS_FT_FI6 13) chain A residue 718-745 type prosite sequence LGSGAFGTVYKGLWIPEGEKVKIPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK source prosite : PS00107 14) chain A residue 833-845 type prosite sequence LVHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV source prosite : PS00109 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) chain A residue 867 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 22) 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 23) 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 24) chain A residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 25) chain A residue 869 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:23774213 source Swiss-Prot : SWS_FT_FI8 26) chain A residue 790 type BINDING sequence T 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 27) 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

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