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1YAC

THE 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE YCAC GENE PRODUCT FROM ESCHERICHIA COLI REVEALS AN OCTAMERIC HYDROLASE OF UNKNOWN SPECIFICITY

Summary for 1YAC
Entry DOI10.2210/pdb1yac/pdb
DescriptorYCAC GENE PRODUCT (2 entities in total)
Functional Keywordsunknown bacterial hydrolase, three layer alpha-beta-alpha sandwich topology, entb homolog, cshase homolog
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight45956.24
Authors
Colovos, C.,Cascio, D.,Yeates, T.O. (deposition date: 1998-07-29, release date: 1999-02-16, Last modification date: 2024-02-14)
Primary citationColovos, C.,Cascio, D.,Yeates, T.O.
The 1.8 A crystal structure of the ycaC gene product from Escherichia coli reveals an octameric hydrolase of unknown specificity.
Structure, 6:1329-1337, 1998
Cited by
PubMed Abstract: The ycaC gene comprises a 621 base pair open reading frame in Escherichia coli. The ycaC gene product (ycaCgp) is uncharacterized and has no assigned function. The closest sequence homologs with an assigned function belong to a family of bacterial hydrolases that catalyze isochorismatase-like reactions, but these have only low sequence similarity to ycaCgp (approximately 20% amino acid identity). The ycaCgp was obtained and identified during crystallization trials of an unrelated E. coli protein with which it co-purified.
PubMed: 9782055
DOI: 10.1016/S0969-2126(98)00132-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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