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2OYS

Crystal Structure of SP1951 protein from Streptococcus pneumoniae in complex with FMN, Northeast Structural Genomics Target SpR27

Summary for 2OYS
Entry DOI10.2210/pdb2oys/pdb
Related1SQS
DescriptorHypothetical protein SP1951, FLAVIN MONONUCLEOTIDE, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsalpha-beta protein, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
Biological sourceStreptococcus pneumoniae
Total number of polymer chains2
Total formula weight57853.26
Authors
Primary citationForouhar, F.,Kuzin, A.,Seetharaman, J.,Lee, I.,Zhou, W.,Abashidze, M.,Chen, Y.,Yong, W.,Janjua, H.,Fang, Y.,Wang, D.,Cunningham, K.,Xiao, R.,Acton, T.B.,Pichersky, E.,Klessig, D.F.,Porter, C.W.,Montelione, G.T.,Tong, L.
Functional insights from structural genomics.
J.Struct.Funct.Genom., 8:37-44, 2007
Cited by
PubMed Abstract: Structural genomics efforts have produced structural information, either directly or by modeling, for thousands of proteins over the past few years. While many of these proteins have known functions, a large percentage of them have not been characterized at the functional level. The structural information has provided valuable functional insights on some of these proteins, through careful structural analyses, serendipity, and structure-guided functional screening. Some of the success stories based on structures solved at the Northeast Structural Genomics Consortium (NESG) are reported here. These include a novel methyl salicylate esterase with important role in plant innate immunity, a novel RNA methyltransferase (H. influenzae yggJ (HI0303)), a novel spermidine/spermine N-acetyltransferase (B. subtilis PaiA), a novel methyltransferase or AdoMet binding protein (A. fulgidus AF_0241), an ATP:cob(I)alamin adenosyltransferase (B. subtilis YvqK), a novel carboxysome pore (E. coli EutN), a proline racemase homolog with a disrupted active site (B. melitensis BME11586), an FMN-dependent enzyme (S. pneumoniae SP_1951), and a 12-stranded beta-barrel with a novel fold (V. parahaemolyticus VPA1032).
PubMed: 17588214
DOI: 10.1007/s10969-007-9018-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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