2npx | pdb_00002npx

NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE

spinqualitylabelsall models 2npx, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2npx is a 1 chain structure with sequence from "enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, NAD NonStd Res: OCS Activity: NADH peroxidase, with EC number 1.11.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NAPE_ENTFA] Peroxidase whose active site is a redox-active cysteine-sulfenic acid. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of the complex between cofactor NADH and the enzyme NADH peroxidase from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been determined by crystal soaking, X-ray data collection, model building of NADH and refinement at 0.24-nm resolution based on the known enzyme structure [Stehle, T., Ahmed, S. A., Claiborne, A. & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344]. Apart from NADH, the catalytic center of the enzyme contains FAD and a cysteine that shuttles between thiolate and sulfenic acid states. Unfortunately, this cysteine was irreversibly oxidized to a cysteine sulfonic acid in the established enzyme structure. Based on the geometry of the catalytic center, we discuss the stabilization of the oxidation-sensitive sulfenic acid and propose a reaction mechanism. NADH binding site and catalysis of NADH peroxidase.,Stehle T, Claiborne A, Schulz GE Eur J Biochem. 1993 Jan 15;211(1-2):221-6. PMID:8425532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NADH peroxidase

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