2NPX
NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE
Summary for 2NPX
| Entry DOI | 10.2210/pdb2npx/pdb |
| Descriptor | NADH PEROXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase(h2o2(a)) |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 1 |
| Total formula weight | 51100.20 |
| Authors | Stehle, T.,Claiborne, A.,Schulz, G.E. (deposition date: 1992-05-29, release date: 1994-01-31, Last modification date: 2024-06-05) |
| Primary citation | Stehle, T.,Claiborne, A.,Schulz, G.E. NADH binding site and catalysis of NADH peroxidase. Eur.J.Biochem., 211:221-226, 1993 Cited by PubMed Abstract: 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. PubMed: 8425532DOI: 10.1111/j.1432-1033.1993.tb19889.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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