1cot | pdb_00001cot

X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1cot, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cot is a 1 chain structure with sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: HEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CY550_PARDE 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 cytochrome c2 (formerly c550) isolated from Paracoccus denitrificans is one of the larger bacterial c-type proteins examined thus far. The molecular structure of this cytochrome has been redetermined and refined to 1.7-A resolution with a crystallographic R-factor of 17.5% for all measured X-ray data. Like other, smaller c-type cytochromes, the molecule consists of five alpha-helices that wrap around the heme group. In addition, this bacterial cytochrome contains two strands of anti-parallel beta-sheet, five Type I turns, and three Type II turns. The present model differs from the originally determined structure in several regions including the N-terminus, the loop delineated by Asp 25 to Lys 31, the region defined by Trp 86 to Val 88, and the C-terminus. A total of 103 water molecules has been positioned into the electron density map. Six of these waters are directly involved in heme binding. X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution.,Benning MM, Meyer TE, Holden HM Arch Biochem Biophys. 1994 May 1;310(2):460-6. PMID:8179333 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures

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