3GQI
Crystal Structure of activated receptor tyrosine kinase in complex with substrates
Summary for 3GQI
Entry DOI | 10.2210/pdb3gqi/pdb |
Related | 3GQL |
Descriptor | Basic fibroblast growth factor receptor 1, Phospholipase C-gamma-1, DECAVANADATE, ... (6 entities in total) |
Functional Keywords | phosphorylated kinase, py-recognition, tandem sh2 domains, atp analog, atp-binding, craniosynostosis, disease mutation, disulfide bond, dwarfism, glycoprotein, heparin-binding, hypogonadotropic hypogonadism, immunoglobulin domain, kallmann syndrome, kinase, membrane, nucleotide-binding, phosphoprotein, receptor, transferase, transmembrane, tyrosine-protein kinase, hydrolase, lipid degradation, sh2 domain, sh3 domain, transducer, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane; Single-pass type I membrane protein: P11362 Cell projection, lamellipodium : P10686 |
Total number of polymer chains | 2 |
Total formula weight | 65292.33 |
Authors | Bae, J.H.,Lew, E.D.,Yuzawa, S.,Tome, F.,Lax, I.,Schlessinger, J. (deposition date: 2009-03-24, release date: 2009-08-18, Last modification date: 2023-11-22) |
Primary citation | Bae, J.H.,Lew, E.D.,Yuzawa, S.,Tome, F.,Lax, I.,Schlessinger, J. The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell(Cambridge,Mass.), 138:514-524, 2009 Cited by PubMed: 19665973DOI: 10.1016/j.cell.2009.05.028 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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