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6Y0K

Sulfite oxidase from Thermus thermophilus with coordinated phosphate

This is a non-PDB format compatible entry.
Summary for 6Y0K
Entry DOI10.2210/pdb6y0k/pdb
DescriptorPutaitve sulfite oxidase, (MOLYBDOPTERIN-S,S)-OXO-MOLYBDENUM, GLYCEROL, ... (5 entities in total)
Functional Keywordsmolybdoenzyme, sulfite oxidase, oxidoreductase
Biological sourceThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Total number of polymer chains1
Total formula weight44409.56
Authors
Djeghader, A.,Soulimane, T. (deposition date: 2020-02-08, release date: 2020-08-05, Last modification date: 2024-01-24)
Primary citationDjeghader, A.,Rossotti, M.,Abdulkarim, S.,Biaso, F.,Gerbaud, G.,Nitschke, W.,Schoepp-Cothenet, B.,Soulimane, T.,Grimaldi, S.
Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase.
Chem.Commun.(Camb.), 56:9850-9853, 2020
Cited by
PubMed Abstract: By combining X-ray crystallography, electron paramagnetic resonance techniques and density functional theory-based modelling, we provide evidence for a direct coordination of the product analogue, phosphate, to the molybdenum active site of a sulfite dehydrogenase. This interaction is mimicking the still experimentally uncharacterized reaction intermediate proposed to arise during the catalytic cycle of this class of enzymes. This work opens new perspectives for further deciphering the reaction mechanism of this nearly ubiquitous class of oxidoreductases.
PubMed: 32716419
DOI: 10.1039/d0cc03634j
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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