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1jfc

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1jfc, resolution 1.05Å

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X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution

Overview

Crystal structures of the nitric oxide reductase cytochrome P450nor, (P450nor) in the ferric resting and the ferrous carbonmonoxy (CO) states, have been determined at 1.00 and 1.05 A resolution, respectively. P450nor, consists of 403 amino-acid residues (46 kDa) and is one of the largest, proteins refined to this resolution so far. The final models have, conventional R factors of 10.2% (ferric resting) and 11.7% (ferrous CO), with mean coordinate errors of 0.028 (ferric resting) and 0.030 A (ferrous, CO) as calculated from inversion of the full positional least-squares, matrix. Owing to the atomic resolution, novel features are found in the, refined structures. Firstly, two orientations of the haem are observed, both in the ferric resting and the ferrous CO states. Secondly, a, disordered water molecule bound to the haem iron is found in the ferric, resting state. In addition, the accurate structures at atomic resolution, enabled the examination of general stereochemical parameters that are, commonly used in refinement cycles of protein structures.

About this Structure

1JFC is a Single protein structure of sequence from Fusarium oxysporum with HEM, CMO and GOL as ligands. Active as Nitric-oxide reductase, with EC number 1.7.99.7 Full crystallographic information is available from OCA.

Reference

X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution., Shimizu H, Park SY, Shiro Y, Adachi S, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):81-9. Epub 2001 Dec, 21. PMID:11752781

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