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7USZ

Human DDAH-1, holo (Zn-bound) form

Summary for 7USZ
Entry DOI10.2210/pdb7usz/pdb
DescriptorN(G),N(G)-dimethylarginine dimethylaminohydrolase 1, ZINC ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordscardiovascular enzyme, proton pump inhibitors, esomeprazole, hydrolase
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight63055.81
Authors
Smith, C.A.,Ghebre, Y.T. (deposition date: 2022-04-26, release date: 2022-05-11, Last modification date: 2023-10-18)
Primary citationSmith, C.A.,Ebrahimpour, A.,Novikova, L.,Farina, D.,Bailey, A.O.,Russell, W.K.,Jain, A.,Saltzman, A.B.,Malovannaya, A.,Prasad, B.V.V.,Hu, L.,Ghebre, Y.T.
Esomeprazole covalently interacts with the cardiovascular enzyme dimethylarginine dimethylaminohydrolase: Insights into the cardiovascular risk of proton pump inhibitors.
Biochim Biophys Acta Gen Subj, 1866:130149-130149, 2022
Cited by
PubMed Abstract: Proton pump inhibitors (PPIs) are widely prescribed drugs for the treatment of gastroesophageal reflux disease (GERD). Several meta-analysis studies have reported associations between prolonged use of PPIs and major adverse cardiovascular events. However, interaction of PPIs with biological molecules involved in cardiovascular health is incompletely characterized. Dimethylarginine dimethylaminohydrolase (DDAH) is a cardiovascular enzyme expressed in cardiomyocytes, and other somatic cell types in one of two isotypes (DDAH1 and DDAH2) to metabolize asymmetric dimethylarginine (ADMA); a cardiovascular risk factor and competitive inhibitor of nitric oxide synthases (NOSs).
PubMed: 35472493
DOI: 10.1016/j.bbagen.2022.130149
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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数据于2025-11-05公开中

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