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4fit
From Proteopedia
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|SITE= <scene name='pdbsite=AVE:Active+Site+HIS+Responsible+For+Forming+The+Transient+Nu+...'>AVE</scene> and <scene name='pdbsite=HNE:HIS+Triad+For+Which+This+Family+Was+Named'>HNE</scene> | |SITE= <scene name='pdbsite=AVE:Active+Site+HIS+Responsible+For+Forming+The+Transient+Nu+...'>AVE</scene> and <scene name='pdbsite=HNE:HIS+Triad+For+Which+This+Family+Was+Named'>HNE</scene> | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Bis(5'-adenosyl)-triphosphatase Bis(5'-adenosyl)-triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.29 3.6.1.29] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-adenosyl)-triphosphatase Bis(5'-adenosyl)-triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.29 3.6.1.29] </span> |
|GENE= FHIT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FHIT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fit OCA], [http://www.ebi.ac.uk/pdbsum/4fit PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4fit RCSB]</span> | ||
}} | }} | ||
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[[Category: putative tumor suppressor]] | [[Category: putative tumor suppressor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:42 2008'' |
Revision as of 02:38, 31 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Gene: | FHIT (Homo sapiens) | ||||||
| Activity: | Bis(5'-adenosyl)-triphosphatase, with EC number 3.6.1.29 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FHIT-APO
Overview
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.
About this Structure
4FIT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 05:38:42 2008
Categories: Bis(5'-adenosyl)-triphosphatase | Homo sapiens | Single protein | Hendrickson, W A. | Klein, M G. | Lima, C D. | Fhit | Fragile histidine triad protein | Histidine triad protein family | Hit protein family | Hydrolase | Nucleotidyl hydrolase | Nucleotidyl transferase | Putative tumor suppressor
