1KPF
PKCI-SUBSTRATE ANALOG
Summary for 1KPF
| Entry DOI | 10.2210/pdb1kpf/pdb |
| Descriptor | PROTEIN KINASE C INTERACTING PROTEIN, ADENOSINE MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | protein kinase inhibitor, pkci-1, hit protein family, histidine triad protein family, nucleotidyl hydrolase, nucleotidyl transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P49773 |
| Total number of polymer chains | 1 |
| Total formula weight | 14065.99 |
| Authors | Lima, C.D.,Klein, M.G.,Hendrickson, W.A. (deposition date: 1997-09-25, release date: 1998-03-25, Last modification date: 2024-10-23) |
| Primary citation | Lima, C.D.,Klein, M.G.,Hendrickson, W.A. Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science, 278:286-290, 1997 Cited by PubMed Abstract: 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. PubMed: 9323207DOI: 10.1126/science.278.5336.286 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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