1gjq
From Proteopedia
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PSEUDOMONAS AERUGINOSA CD1 NITRITE REDUCTASE REDUCED CYANIDE COMPLEX
Overview
Cyanide binding to fully reduced Pseudomonas aeruginosa cd(1) nitrite, reductase (Pa cd(1) NiR) has been investigated for the wild-type enzyme, and a site-directed mutant in which the active-site His369 was replaced by, Ala. This mutation reduces the affinity toward cyanide (by approximately, 13-fold) and especially decreases the rate of binding of cyanide to the, reduced d(1) heme (by approximately 100-fold). The crystal structure of, wild-type reduced Pa cd(1) NiR saturated with cyanide was determined to a, resolution of 2.7 A. Cyanide binds to the iron of the d(1) heme, with an, Fe-C-N angle of 168 degrees for both subunits of the dimer and only His369, is within hydrogen bonding distance of the nitrogen atom of the ligand., These results suggest that in Pa cd(1) NiR the invariant ... [(full description)]
About this Structure
1GJQ is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with CYN, HEC and DHE as [ligands]. Active as [Transferred entry: 1.7.2.1], with EC number [1.9.3.2]. Structure known Active Site: HEA. Full crystallographic information is available from [OCA].
Reference
Cyanide binding to cd(1) nitrite reductase from Pseudomonas aeruginosa: role of the active-site His369 in ligand stabilization., Sun W, Arese M, Brunori M, Nurizzo D, Brown K, Cambillau C, Tegoni M, Cutruzzola F, Biochem Biophys Res Commun. 2002 Feb 15;291(1):1-7. PMID:11829453
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