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3FIT

FHIT (FRAGILE HISTIDINE TRIAD PROTEIN) IN COMPLEX WITH ADENOSINE/SULFATE AMP ANALOG

Summary for 3FIT
Entry DOI10.2210/pdb3fit/pdb
DescriptorFRAGILE HISTIDINE PROTEIN, beta-D-fructofuranose, SULFATE ION, ... (5 entities in total)
Functional Keywordsfhit, fragile histidine triad protein, putative human tumor suppressor, advanced photon source, aps, hit protein family, pkci, complex (chromosomal translocation-ade), complex (chromosomal translocation-ade) complex, complex (chromosomal translocation/ade)
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight17699.49
Authors
Lima, C.D.,D'Amico, K.L.,Naday, I.,Rosenbaum, G.,Westbrook, E.M.,Hendrickson, W.A. (deposition date: 1997-05-17, release date: 1997-11-19, Last modification date: 2024-11-06)
Primary citationLima, C.D.,D'Amico, K.L.,Naday, I.,Rosenbaum, G.,Westbrook, E.M.,Hendrickson, W.A.
MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family.
Structure, 5:763-774, 1997
Cited by
PubMed Abstract: The fragile histidine triad (FHIT) protein is a member of the large and ubiquitous histidine triad (HIT) family of proteins. It is expressed from a gene located at a fragile site on human chromosome 3, which is commonly disrupted in association with certain cancers. On the basis of the genetic evidence, it has been postulated that the FHIT protein may function as a tumor suppressor, implying a role for the FHIT protein in carcinogenesis. The FHIT protein has dinucleoside polyphosphate hydrolase activity in vitro, thus suggesting that its role in vivo may involve the hydrolysis of a phosphoanhydride bond. The structural analysis of FHIT will identify critical residues involved in substrate binding and catalysis, and will provide insights into the in vivo function of HIT proteins.
PubMed: 9261067
DOI: 10.1016/S0969-2126(97)00231-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2025-12-03公开中

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