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1ux8
From Proteopedia
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X-RAY STRUCTURE OF TRUNCATED OXYGEN-AVID HAEMOGLOBIN FROM BACILLUS SUBTILIS
Overview
The group II truncated hemoglobin from Bacillus subtilis has been cloned, expressed, purified, and characterized. B. subtilis truncated hemoglobin, is a monomeric protein endowed with an unusually high oxygen affinity (in, the nanomolar range) such that the apparent thermodynamic binding constant, for O2 exceeds that for CO by 1 order of magnitude. The kinetic basis of, the high oxygen affinity resides mainly in the very slow rate of ligand, release. The extremely stable ferrous oxygenated adduct is resistant to, oxidation, which can be achieved only with oxidant in large excess, e.g., ferricyanide in 50-fold molar excess. The three-dimensional crystal, structure of the cyano-Met derivative was determined at 2.15 A resolution., Although the overall fold resembles that of other truncated ... [(full description)]
About this Structure
1UX8 is a [Single protein] structure of sequence from [Bacillus subtilis] with CYN, CL and HEM as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties., Giangiacomo L, Ilari A, Boffi A, Morea V, Chiancone E, J Biol Chem. 2005 Mar 11;280(10):9192-202. Epub 2004 Dec 7. PMID:15590662
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