1ad5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the haematopoietic cell kinase Hck has been | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: tyrosine-protein kinase]] | [[Category: tyrosine-protein kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:19 2008'' |
Revision as of 09:43, 21 February 2008
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SRC FAMILY KINASE HCK-AMP-PNP COMPLEX
Overview
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.
About this Structure
1AD5 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of the Src family tyrosine kinase Hck., Sicheri F, Moarefi I, Kuriyan J, Nature. 1997 Feb 13;385(6617):602-9. PMID:9024658
Page seeded by OCA on Thu Feb 21 11:43:19 2008
Categories: Homo sapiens | Single protein | Transferase | Kuriyan, J. | Moarefi, I. | Sicheri, F. | ANP | CA | Phosphorylation | Sh2 | Sh3 | Signal transduction | Tyrosine-protein kinase
