3GQL
Crystal Structure of activated receptor tyrosine kinase in complex with substrates
Summary for 3GQL
Entry DOI | 10.2210/pdb3gql/pdb |
Related | 3GQI |
Descriptor | Basic fibroblast growth factor receptor 1, (E)-[4-(3,5-difluorophenyl)-3H-pyrrolo[2,3-b]pyridin-3-ylidene](3-methoxyphenyl)methanol (3 entities in total) |
Functional Keywords | phosphorylated kinase, activation, 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, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane; Single-pass type I membrane protein: P11362 |
Total number of polymer chains | 3 |
Total formula weight | 112965.65 |
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: 2024-02-21) |
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 (2.8 Å) |
Structure validation
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