Tyrosine Kinase: Hck

	Select: Protein Ligands All Rotate: X 90° X -90° Y 90° Y -90°	Distances: Ca²⁺ Asn391 Thr338 Lys295 Reset The rotate buttons act on the entire structure. Remove the distance monitors with a second click.
	The ATP binding pocket with three "close" residues (<3.2 Å) shown as Ball & Stick. The van der Waals surface of the binding pocket (atoms within 5.5 Å of ATP) shown as Ball & Stick with dot surface. The Src-homology domains: SH3 (yellow) and SH2 (green). Src Family Tyrosine Kinase: Hck Overall architecture of the haematopoietic cell kinase (Hck). One subunit of the homodimer is shown as Ribbons with Structure coloring. The ligands (AMPPnP & Ca²⁺) are Spacefill, colored CPK. Use the buttons to the right of the image to select portions of the structure for display or coloring in the Chime menu.

The coordinates are from 1ad5.pdb (subunit A only). Sicheri, F. et al. (1997) "Crystal structure of the Src family tyrosine kinase Hck"Nature 385, 602.; and Xu, W. et al. (1997) "Three-dimensional structure of the tyrosine kinase c-Src"Nature 385, 595.

Additional notes on the Hck structure:

Crystals grown at pH 6.5 in 0.15 m Ca acetate.

Resolution: 2.9-2.6 Å; R-factor: 0.23.

Domains.

SH3: residues 85-145, peptide binding.
SH2: residues 149-240, peptide binding.
Kinase: residues 250-526.

Homology features.

Overall fold similar to nine other protein kinases
P244-W254 is lefthanded polyproline type II helix.

E310 swung out and away from K295 (14 Å).

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