1paz

REFINEMENT OF THE STRUCTURE OF PSEUDOAZURIN FROM ALCALIGENES FAECALIS S-6 AT 1.55 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1paz, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1paz is a 1 chain structure with sequence from Alcfa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AZUP_ALCFA] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase. 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 crystal structure of the redox protein pseudoazurin (123 amino acid residues; molecular weight 13,000 daltons) from Alcaligenes faecalis has been refined by fast Fourier restrained least-squares minimization. Cycles of rebuilding were carried out to escape from local minima. Individual isotropic temperature factor values were refined separately for all atoms. The R factor was reduced from 0.400 (for 2647 reflections in the 6.0-2.8 A resolution range) to 0.180 (for all 19,770 reflections in the 9.0-1.55 A resolution range) with a final estimated accuracy in atomic positions of 0.15 A. The final model comprises 917 protein atoms and 93 solvent molecules. The root-mean-square shift of the main-chain atoms between the final and the initial model is 0.94 A (maximum shift 1.8 A). Most of the larger shifts were the result of rebuilding on the graphics system. The average atomic temperature factor, B, is 23.0 A2 for all atoms. Side-chain atoms with high B values were omitted, and their positions checked from difference maps. The three carboxy-terminal residues were omitted from the final model as no single conformation could be assigned from the observed electron density. All other protein atoms were included. Refinement of the structure of pseudoazurin from Alcaligenes faecalis S-6 at 1.55 A resolution.,Petratos K, Dauter Z, Wilson KS Acta Crystallogr B. 1988 Dec 1;44 ( Pt 6):628-36. PMID:3271558 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pseudoazurin

Proteopedia Page Contributors and Editors (what is this?)

OCA