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7WRK

Structure of hypothetical protein TTHA1873 from Thermus thermophilus

Summary for 7WRK
Entry DOI10.2210/pdb7wrk/pdb
Descriptorhypothetical protein TTHA1873, CALCIUM ION (3 entities in total)
Functional Keywordsunknown function
Biological sourceThermus thermophilus HB8
Total number of polymer chains1
Total formula weight18556.34
Authors
Yuvaraj, I.,Santosh, K.C.,Sekar, K. (deposition date: 2022-01-27, release date: 2022-03-09, Last modification date: 2024-05-29)
Primary citationYuvaraj, I.,Chaudhary, S.K.,Jeyakanthan, J.,Sekar, K.
Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.
Acta Crystallogr.,Sect.F, 78:338-346, 2022
Cited by
PubMed Abstract: The crystal structure of an uncharacterized hypothetical protein, TTHA1873 from Thermus thermophilus, has been determined by X-ray crystallography to a resolution of 1.78 Å using the single-wavelength anomalous dispersion method. The protein crystallized as a dimer in two space groups: P422 and P622. Structural analysis of the hypothetical protein revealed that the overall fold of TTHA1873 has a β-sandwich jelly-roll topology with nine β-strands. TTHA1873 is a dimeric metal-binding protein that binds to two Ca ions per chain, with one on the surface and the other stabilizing the dimeric interface of the two chains. A structural homology search indicates that the protein has moderate structural similarity to one domain of cell-surface proteins or agglutinin receptor proteins. Red blood cells showed visible agglutination at high concentrations of the hypothetical protein.
PubMed: 36048084
DOI: 10.1107/S2053230X22008457
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.78 Å)
Structure validation

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