1kpe

PKCI-TRANSITION STATE ANALOG

spinqualitylabelsall models 1kpe, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kpe is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: ACE, ADW Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HINT1_HUMAN Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics. Structure-based analysis of catalysis and substrate definition in the HIT protein family.,Lima CD, Klein MG, Hendrickson WA Science. 1997 Oct 10;278(5336):286-90. PMID:9323207 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histidine triad nucleotide-binding protein 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA