1AD5
SRC FAMILY KINASE HCK-AMP-PNP COMPLEX
Summary for 1AD5
| Entry DOI | 10.2210/pdb1ad5/pdb |
| Descriptor | HAEMATOPOETIC CELL KINASE HCK, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total) |
| Functional Keywords | tyrosine-protein kinase, transferase, signal transduction, sh2, sh3, phosphorylation |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform p59-HCK: Membrane; Lipid-anchor. Isoform p60-HCK: Membrane; Lipid-anchor: P08631 |
| Total number of polymer chains | 2 |
| Total formula weight | 101781.40 |
| Authors | Sicheri, F.,Moarefi, I.,Kuriyan, J. (deposition date: 1997-02-20, release date: 1997-05-15, Last modification date: 2024-10-23) |
| Primary citation | Sicheri, F.,Moarefi, I.,Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck. Nature, 385:602-609, 1997 Cited by PubMed Abstract: The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 A resolution. Inhibition of enzymatic activity is a consequence of intramolecular interactions of the enzyme's Src-homology domains SH2 and SH3, with concomitant displacement of elements of the catalytic domain. The conformation of the active site has similarities with that of inactive cyclin-dependent protein kinases. PubMed: 9024658DOI: 10.1038/385602a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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